SSB_VIBPA
ID SSB_VIBPA Reviewed; 176 AA.
AC Q87LA3;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssb; OrderedLocusNames=VP2709;
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: Plays an important role in DNA replication, recombination and
CC repair. Binds to ssDNA and to an array of partner proteins to recruit
CC them to their sites of action during DNA metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00984}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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; BA000031; BAC60972.1; -; Genomic_DNA.
DR RefSeq; NP_799088.1; NC_004603.1.
DR RefSeq; WP_005466625.1; NC_004603.1.
DR AlphaFoldDB; Q87LA3; -.
DR SMR; Q87LA3; -.
DR STRING; 223926.28807719; -.
DR EnsemblBacteria; BAC60972; BAC60972; BAC60972.
DR GeneID; 1190254; -.
DR KEGG; vpa:VP2709; -.
DR PATRIC; fig|223926.6.peg.2605; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_6; -.
DR OMA; GQMQERT; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR PIRSF; PIRSF002070; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Reference proteome.
FT CHAIN 1..176
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096137"
FT DOMAIN 6..111
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DNA_BIND 55..61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 114..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 171..176
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 124..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 19564 MW; BC3FB8C181951EB7 CRC64;
MASRGINKVI LVGNLGNDPE IRYMPNGGAV ANITIATSES WRDKATGEQR EKTEWHRVVL
FGKLAEVAGE YLRKGSQVYV EGQLQTRKWQ DQSGQDRYST EVVVQGFNGV MQMLGGRAQG
GAPAMGGQQQ QQGGWGQPQQ PAQQQYNAPQ QQQQAPQQPQ QQYNEPPMDF DDDIPF