In Silico Approach on Structural and Functional Characterization of Heat shock protein from Sulfobacillus acidophilus

In Silico Approach on Structural and Functional Characterization of Heat shock protein from Sulfobacillus acidophilus | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article In Silico Approach on Structural and Functional Characterization of Heat shock protein from Sulfobacillus acidophilus Pritish Mitra, Sabyasachi Chatterjee This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-5333465/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract The 70 kDa heat shock proteins (Hsp70s) are highly conserved and ubiquitous molecular chaperones. Hsp70 proteins are intimately involved in different biological activities including maintaining protein homeostasis and resisting environmental stress for survival. Characterizations of eukaryotic Hsp70s with diverse functions are well established but investigations needed for prokaryotes. For better understanding, the sequences of Sulfobacillus acidophilus were retrieved from UniProt. Retrieved Hsp70 proteins were renamed as SaHsp70s and performed an in-silico analysis of Hsp70 proteins to identify sequential, structural properties and functional attributes. The in-silico characterization of Hsp70 proteins revealed that they are acidic, mostly thermostable globular protein with NAD(P)-binding Rossmann-folding. Molecular mass of SaHsp70s ranged from 31.9 to 68.5 kDa and mainly localized in the cytoplasm. Phylogeny revealed the evolutionary distance and relationship among retrieved proteins. Domain analyzed only SaHsp70-1, SaHsp70-3and SaHsp70-14 have actual conserved domain for Hsp70 and share the same clade on phylogenetic tree. Major part of each protein was abundant with α-helix and random coil which make it thermally stable and suitable for interacting with other proteins. SAVES and ProSA server proves the reliability, stability and consistency tertiary structure of SaHsp70s. Functional analysis was done in terms of membrane protein topology, PPI network generation, active and proteolytic cleavage sites prediction, conserved motif and domain detection. Active site predicted Asp, Lys and Glu act as catalytic residue, are important for metal ions binding. Findings suggested that SaHsp70 proteins play central role various complex cellular functions like stress mitigation, thermal stability and related developmental processes. In-silico analysis SaHsp70 protein Sulfobacillus acidophilus Sequential and structural properties Phylogeny Full Text Additional Declarations No competing interests reported. Supplementary Files Supplementaryfile.docx Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-5333465","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":370618651,"identity":"3c8ca451-7258-4eae-b931-ac9ea30161e1","order_by":0,"name":"Pritish Mitra","email":"","orcid":"","institution":"Ramananda College","correspondingAuthor":false,"prefix":"","firstName":"Pritish","middleName":"","lastName":"Mitra","suffix":""},{"id":370618652,"identity":"05a4e1b1-bed8-4cb3-9b6c-35982fc85df5","order_by":1,"name":"Sabyasachi Chatterjee","email":"data:image/png;base64,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","orcid":"","institution":"Ramananda College","correspondingAuthor":true,"prefix":"","firstName":"Sabyasachi","middleName":"","lastName":"Chatterjee","suffix":""}],"badges":[],"createdAt":"2024-10-25 15:38:04","currentVersionCode":1,"declarations":{"humanSubjects":false,"vertebrateSubjects":false,"conflictsOfInterestStatement":false,"humanSubjectEthicalGuidelines":false,"humanSubjectConsent":false,"humanSubjectClinicalTrial":false,"humanSubjectCaseReport":false,"vertebrateSubjectEthicalGuidelines":false},"doi":"10.21203/rs.3.rs-5333465/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-5333465/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":70278306,"identity":"86e6d01d-59e3-471b-94cf-15af68900a14","added_by":"auto","created_at":"2024-12-01 13:16:49","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":911340,"visible":true,"origin":"","legend":"","description":"","filename":"Manuscript.pdf","url":"https://assets-eu.researchsquare.com/files/rs-5333465/v1_covered_1ec61701-ae59-4658-a6ab-5c9c5ec4e45b.pdf"},{"id":68358340,"identity":"bd029c7f-9725-4119-87b3-60d6fc490294","added_by":"auto","created_at":"2024-11-06 11:49:29","extension":"docx","order_by":1,"title":"","display":"","copyAsset":false,"role":"supplement","size":1300541,"visible":true,"origin":"","legend":"","description":"","filename":"Supplementaryfile.docx","url":"https://assets-eu.researchsquare.com/files/rs-5333465/v1/1483d423800609a348916470.docx"}],"financialInterests":"No competing interests reported.","formattedTitle":"In Silico Approach on Structural and Functional Characterization of Heat shock protein from Sulfobacillus acidophilus","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"In-silico analysis, SaHsp70 protein, Sulfobacillus acidophilus, Sequential and structural properties, Phylogeny","lastPublishedDoi":"10.21203/rs.3.rs-5333465/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-5333465/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"\u003cp\u003eThe 70 kDa heat shock proteins (Hsp70s) are highly conserved and ubiquitous molecular chaperones. Hsp70 proteins are intimately involved in different biological activities including maintaining protein homeostasis and resisting environmental stress for survival. Characterizations of eukaryotic Hsp70s with diverse functions are well established but investigations needed for prokaryotes. For better understanding, the sequences of \u003cem\u003eSulfobacillus acidophilus\u003c/em\u003e were retrieved from UniProt. Retrieved Hsp70 proteins were renamed as SaHsp70s and performed an \u003cem\u003ein-silico\u003c/em\u003e analysis of Hsp70 proteins to identify sequential, structural properties and functional attributes. The \u003cem\u003ein-silico\u003c/em\u003e characterization of Hsp70 proteins revealed that they are acidic, mostly thermostable globular protein with NAD(P)-binding Rossmann-folding. Molecular mass of SaHsp70s ranged from 31.9 to 68.5 kDa and mainly localized in the cytoplasm. Phylogeny revealed the evolutionary distance and relationship among retrieved proteins. Domain analyzed only SaHsp70-1, SaHsp70-3and SaHsp70-14 have actual conserved domain for Hsp70 and share the same clade on phylogenetic tree. Major part of each protein was abundant with α-helix and random coil which make it thermally stable and suitable for interacting with other proteins. SAVES and ProSA server proves the reliability, stability and consistency tertiary structure of SaHsp70s. Functional analysis was done in terms of membrane protein topology, PPI network generation, active and proteolytic cleavage sites prediction, conserved motif and domain detection. Active site predicted Asp, Lys and Glu act as catalytic residue, are important for metal ions binding. Findings suggested that SaHsp70 proteins play central role various complex cellular functions like stress mitigation, thermal stability and related developmental processes.\u003c/p\u003e","manuscriptTitle":"In Silico Approach on Structural and Functional Characterization of Heat shock protein from Sulfobacillus acidophilus","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2024-11-06 11:49:24","doi":"10.21203/rs.3.rs-5333465/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"0398fb70-fb94-43e0-a326-b02efe12ece0","owner":[],"postedDate":"November 6th, 2024","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[],"tags":[],"updatedAt":"2024-12-14T15:00:34+00:00","versionOfRecord":[],"versionCreatedAt":"2024-11-06 11:49:24","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-5333465","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-5333465","identity":"rs-5333465","version":["v1"]},"buildId":"qtupq5eGEP_6zYnWcrvyt","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}