ID   PRIB_VIBPA              Reviewed;         100 AA.
AC   Q87L73;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=VP2739;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC       (PAS). {ECO:0000255|HAMAP-Rule:MF_00720}.
CC   -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, PriB,
CC       PriC, DnaB and DnaT. Upon transient interaction with DnaG it forms the
CC       primosome. {ECO:0000255|HAMAP-Rule:MF_00720}.
CC   -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00720}.
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DR   EMBL; BA000031; BAC61002.1; -; Genomic_DNA.
DR   RefSeq; NP_799118.1; NC_004603.1.
DR   RefSeq; WP_005467185.1; NC_004603.1.
DR   AlphaFoldDB; Q87L73; -.
DR   SMR; Q87L73; -.
DR   STRING; 223926.28807749; -.
DR   PRIDE; Q87L73; -.
DR   EnsemblBacteria; BAC61002; BAC61002; BAC61002.
DR   GeneID; 1190289; -.
DR   KEGG; vpa:VP2739; -.
DR   PATRIC; fig|223926.6.peg.2636; -.
DR   eggNOG; COG2965; Bacteria.
DR   HOGENOM; CLU_166075_0_0_6; -.
DR   OMA; CQMPVII; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00720; PriB; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000424; Primosome_PriB/ssb.
DR   InterPro; IPR023646; Prisomal_replication_PriB.
DR   Pfam; PF00436; SSB; 1.
DR   PIRSF; PIRSF003135; Primosomal_n; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR04418; PriB_gamma; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Primosome; Reference proteome.
FT   CHAIN           1..100
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_0000199065"
FT   DOMAIN          1..100
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   100 AA;  11031 MW;  C311D4A689FF71DD CRC64;
     MTNRMELSGT IAKPPIRSKS PGGIEHCRFW LEHRSTVIEA DLPRQVYCRM PVVVSGLRSQ
     AITQNLVQGS NIKVSGFVAY QTGRNGVGKL VLHADNITQI