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High levels of Mg(2+) (13 mM MgCl(2+)) or incubation with DNase allow holoenzyme reassembly, suggesting it is DNA bound to RecB that prevents reassembly (PubMed:10197988)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1653221"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4275917"}],"value":"(Microbial infection) RecBCD is inhibited by the lambda virus gam protein (both GamL and GamS isoforms); in vitro a short preincubation prior to adding DNA results in maximal inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01487"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15538360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1618858"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18668125"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3526335"}],"value":"Heterotrimer of RecB, RecC and RecD. 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PriB"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1646811"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1856227"}],"value":"Primosomal replication protein n"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00720"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1646811"}],"value":"priB"},"orderedLocusNames":[{"value":"b4201"},{"value":"JW4159"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11532137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15383524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16188886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16899446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1856227"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20156448"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22636770"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34423481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37169801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8366072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663106"}],"value":"Involved in the restart of stalled replication forks, which reloads the replicative helicase (DnaB) on sites other than the origin of replication; the PriA-PriB pathway is the major replication restart pathway (PubMed:11532137, PubMed:37169801, PubMed:22636770). There are several restart pathways, the PriA-PriB pathway is subdivided into 2 distinct pathways (PubMed:34423481). priB and priC have redundant roles in the cell (PubMed:10540288). During primosome assembly it facilitates complex formation between PriA and DnaT on DNA; stabilizes PriA on DNA, presumably by preventing or inhibiting PriA DNA translocation activity (PubMed:8663104, PubMed:8663105, PubMed:8663106). Forms a branched DNA-PriA-PriB complex when the lagging strand is single-stranded (ss)DNA (PubMed:16188886). Binds ssDNA in the presence and absence of ssDNA DNA-binding protein (SSB), does not bind branched structures (PubMed:8366072, PubMed:16188886). DNA binding, forming spiral filaments on ssDNA, is cooperative (PubMed:16899446). Stimulates the helicase activity of PriA (PubMed:16188886, PubMed:37169801, PubMed:34423481). The homodimer binds 12 nucleotides of ssDNA (PubMed:20156448). Binds homo-pyrimidine tracts better than homo-purine tracts (PubMed:15383524, PubMed:20156448)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36326440"}],"value":"Genetic interactions among priB, dam, lexA, nagC, polA, rdgB, rdgB, rep and uup link the PriA-PriB replication restart pathway to DNA double-strand break repair"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00720"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15383524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15530361"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16899446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17588514"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20156448"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25265331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30659961"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37169801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6454139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8366072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663106"}],"value":"Homodimer (PubMed:20156448, PubMed:15383524, PubMed:15530361, PubMed:16899446, PubMed:17588514, PubMed:30659961, PubMed:37169801). Primosome assembly occurs via a 'hand-off' mechanism. PriA binds to replication forks, subsequently PriB then DnaT bind; DnaT then displaces ssDNA to generate the helicase loading substrate, which allows DnaC to load helicase DnaB onto the fork (PubMed:8663104, PubMed:8663105, PubMed:8663106, PubMed:17588514, PubMed:25265331, PubMed:30659961). ssDNA is displaced from the PriB-ssDNA complex by DnaT (PubMed:25265331, PubMed:30659961). In a PriA-PriB-replication fork structure, movement of the PriA CRR domain exposes a surface to which PriB binds and contacts ssDNA emerging from the PriA pore (PubMed:37169801). Binds PriA; binding is improved in the presence of ssDNA (PubMed:8663106, PubMed:17588514, PubMed:37169801). Weakly binds DnaT; binding is improved in the presence of ssDNA; as DnaT levels increase PriB dissociates from ssDNA (PubMed:17588514, PubMed:25265331, PubMed:30659961). Component of the replication restart primosome, which is composed of PriA, PriB, PriC, DnaB and DnaT; DnaG primase associates transiently with this complex (PubMed:6454139, PubMed:8366072, PubMed:8663104, PubMed:8663105, PubMed:17588514). Component of the preprimosomal complex composed of one monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB and one hexamer of DnaB (PubMed:8663105)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P07013","intActId":"EBI-1125223"},"interactantTwo":{"uniProtKBAccession":"P0A8J2","geneName":"dnaT","intActId":"EBI-549621"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07013","intActId":"EBI-1125223"},"interactantTwo":{"uniProtKBAccession":"P17888","geneName":"priA","intActId":"EBI-552050"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07013","intActId":"EBI-1125223"},"interactantTwo":{"uniProtKBAccession":"P07013","geneName":"priB","intActId":"EBI-1125223"},"numberOfExperiments":4,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20005847"}],"value":"Induced by hydroxyurea"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15383524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15530361"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16899446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17588514"}],"value":"Displays high structural similarity to the ssDNA-binding domains of single-stranded binding protein (SSB) (PubMed:15383524, PubMed:15530361). Unlike SSB binds ssDNA in a shallow groove on its surface where DNA contacts both monomers (PubMed:16899446). The L45 loop (residues 82-89) plays a significant role in ssDNA binding (PubMed:16899446). PriB's binding sites for PriA, DnaT and ssDNA overlap on the surface of PriB (PubMed:17588514)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15383524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15530361"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1TXY"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1V1Q"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2CCZ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5WQV"}],"value":"An intersubunit disulfide bond is seen in some crystals (PubMed:15383524, PubMed:15530361)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10540288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11532137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22636770"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36326440"}],"value":"Called priB302; no growth phenotype, 2-fold decrease in recombination proficiency (PubMed:10540288, PubMed:11532137, PubMed:22636770). Inviable at 10 ng/ml ciprofloxacin (PubMed:36326440). Resumption of DNA synthesis after arrest of DNA replication (upon UV treatment) is slower than wild-type, no change in survival after UV treatment (PubMed:22636770). A double priB-priC deletion causes a drastic reduction in cell growth and/or viability (PubMed:10540288). Strongly reduced UV resistance and greatly increased SOS induction; when associated with 'R-230', 'Y-479' or to a lesser extent 'P-557' in priA (PubMed:11532137). Synthetically lethal in combination with a polA, priC, rep or lexA deletion (PubMed:36326440). Double deletions with dam, nagC, rdgB, rdgC or uup are seriously disadvantageous to cells (PubMed:36326440)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00720"}],"value":"Belongs to the PriB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1856227"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Replication restart protein PriB","featureId":"PRO_0000199050"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"SSB","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00720"}]},{"type":"Motif","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"L45 loop","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16899446"}]},{"type":"Disulfide bond","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Interchain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15383524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15530361"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"1V1Q"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1TXY"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2CCZ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5WQV"}]},{"type":"Mutagenesis","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"No change in ssDNA binding, decreased displacement of PriB from ssDNA by DnaT fragment, greatly decreased binding to DnaT fragment (residues 1-88). 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