SSB_RICTY
ID SSB_RICTY Reviewed; 152 AA.
AC Q68Y11;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=RT0824;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04279.1; -; Genomic_DNA.
DR RefSeq; WP_011191253.1; NC_006142.1.
DR AlphaFoldDB; Q68Y11; -.
DR SMR; Q68Y11; -.
DR STRING; 257363.RT0824; -.
DR EnsemblBacteria; AAU04279; AAU04279; RT0824.
DR KEGG; rty:RT0824; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_5; -.
DR OMA; GNCIGRF; -.
DR OrthoDB; 1942216at2; -.
DR Proteomes; UP000000604; Chromosome.
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.
FT CHAIN 1..152
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000286493"
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 117..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..152
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 17452 MW; 2592686F768A2D49 CRC64;
MAGSLNKVIL IGNVGRDPEI RTTGEGKKII NLSLATTETW KDRITSERKE RTEWHRVVIF
SEGLVSIVER YVTKGSKLYI EGSLQTRKWN DNSGQEKYTT EVVLQNFNSQ LILLDNKNSN
NHTQGSGHNE YKYPEIKNHS FDHSDLDDEI PF
