PRIB_SALTY
ID PRIB_SALTY Reviewed; 104 AA.
AC Q8ZK82;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=STM4392;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC (PAS). During primosome assembly it facilitates the complex formation
CC between PriA and DnaT. {ECO:0000255|HAMAP-Rule:MF_00720}.
CC -!- SUBUNIT: Component of the preprimosomal complex composed of one monomer
CC of PriC and DnaT, two monomers of PriA, two dimers of PriB and one
CC hexamer of DnaB. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL23212.1; -; Genomic_DNA.
DR RefSeq; NP_463253.1; NC_003197.2.
DR RefSeq; WP_001519453.1; NC_003197.2.
DR AlphaFoldDB; Q8ZK82; -.
DR SMR; Q8ZK82; -.
DR STRING; 99287.STM4392; -.
DR PaxDb; Q8ZK82; -.
DR EnsemblBacteria; AAL23212; AAL23212; STM4392.
DR GeneID; 1255918; -.
DR GeneID; 66758616; -.
DR KEGG; stm:STM4392; -.
DR PATRIC; fig|99287.12.peg.4617; -.
DR HOGENOM; CLU_166075_0_0_6; -.
DR OMA; CQMPVII; -.
DR PhylomeDB; Q8ZK82; -.
DR BioCyc; SENT99287:STM4392-MON; -.
DR Proteomes; UP000001014; Chromosome.
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 CDD; cd04496; SSB_OBF; 1.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..104
FT /note="Primosomal replication protein N"
FT /id="PRO_0000199061"
FT DOMAIN 2..101
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ SEQUENCE 104 AA; 11414 MW; 9C69E7288F735AA2 CRC64;
MTNRLALSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ
AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD