SSB_COXBU
ID SSB_COXBU Reviewed; 158 AA.
AC Q83EP4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CBU_0271;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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}.
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DR EMBL; AE016828; AAO89829.1; -; Genomic_DNA.
DR RefSeq; NP_819315.1; NC_002971.3.
DR RefSeq; WP_005771486.1; NC_002971.4.
DR PDB; 3TQY; X-ray; 2.60 A; A/B/C/D=1-155.
DR PDBsum; 3TQY; -.
DR AlphaFoldDB; Q83EP4; -.
DR SMR; Q83EP4; -.
DR STRING; 227377.CBU_0271; -.
DR DNASU; 1208152; -.
DR EnsemblBacteria; AAO89829; AAO89829; CBU_0271.
DR GeneID; 1208152; -.
DR KEGG; cbu:CBU_0271; -.
DR PATRIC; fig|227377.7.peg.265; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_6; -.
DR OMA; SGSVKCR; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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 GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Reference proteome.
FT CHAIN 1..158
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096035"
FT DOMAIN 5..110
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 109..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 153..158
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 115..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..17
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 28..41
FT /evidence="ECO:0007829|PDB:3TQY"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:3TQY"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 76..89
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3TQY"
FT STRAND 95..108
FT /evidence="ECO:0007829|PDB:3TQY"
SQ SEQUENCE 158 AA; 17437 MW; FBCDED663A1C03DC CRC64;
MARGVNKVIL IGNLGQDPEV RYTPNGNAVA NVTLATSTTW RDKQTGELQE RTEWHRIAFF
NRLAEIVGEY LRKGSKIYIE GSLRTRKWQD KNGVDRYTTE IIANEMHMLD NRGGGNSGNY
GNHSEGGASN KQSAPTSSQT PTAGDDSSVA DFDDDIPF
