SSB_BRUA2
ID SSB_BRUA2 Reviewed; 168 AA.
AC Q2YPX7; Q07432; Q57D35;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=BAB1_1126;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8225607; DOI=10.1128/iai.61.12.5339-5344.1993;
RA Zhu Y., Oliveira S.C., Splitter G.A.;
RT "Isolation of Brucella abortus ssb and uvrA genes from a genomic library by
RT use of lymphocytes as probes.";
RL Infect. Immun. 61:5339-5344(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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}.
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DR EMBL; L10843; AAA16818.1; -; Unassigned_DNA.
DR EMBL; AM040264; CAJ11082.1; -; Genomic_DNA.
DR PIR; I40352; I40352.
DR RefSeq; WP_002964231.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YPX7; -.
DR SMR; Q2YPX7; -.
DR STRING; 359391.BAB1_1126; -.
DR EnsemblBacteria; CAJ11082; CAJ11082; BAB1_1126.
DR GeneID; 3787774; -.
DR KEGG; bmf:BAB1_1126; -.
DR PATRIC; fig|359391.11.peg.27; -.
DR HOGENOM; CLU_078758_0_1_5; -.
DR OMA; GQMQERT; -.
DR PhylomeDB; Q2YPX7; -.
DR Proteomes; UP000002719; Chromosome I.
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 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..168
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096014"
FT DOMAIN 5..111
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DNA_BIND 54..60
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 113..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..168
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 129..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 168 AA; 18398 MW; ECDDE21EDDDD7886 CRC64;
MAGSVNKVIL VGNLGADPEI RRLNSGDMVA NLRIATSESW RDRQTGERKD RTEWHSVVIF
NENLAKVAEQ YLKKGAKVYI EGALQTRKWQ DQNGNDRYSK EIVLQKFRGE LQMLDSRSEG
GEGRSFGGGG NRNQMSDYSG GGGDFGSSGP SSGSSGGFSR DLDDEIPF
