PRIB_SHIFL
ID PRIB_SHIFL Reviewed; 104 AA.
AC P67677; Q7UAK4; Q8XDI0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720};
GN OrderedLocusNames=SF4354.1, S4626;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAP19555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014073; AAP19555.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001296681.1; NZ_WPGW01000113.1.
DR AlphaFoldDB; P67677; -.
DR SMR; P67677; -.
DR EnsemblBacteria; AAP19555; AAP19555; S4626.
DR GeneID; 66671886; -.
DR KEGG; sfx:S4626; -.
DR PATRIC; fig|623.156.peg.2941; -.
DR HOGENOM; CLU_166075_0_0_6; -.
DR OMA; CQMPVII; -.
DR OrthoDB; 1942216at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000199063"
FT DOMAIN 2..101
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ SEQUENCE 104 AA; 11472 MW; 6622ED9395C2F1B8 CRC64;
MTNRLVLSGT VCRTPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ
AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD