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Database: UniProt
Entry: B4R9P1_PHEZH
LinkDB: B4R9P1_PHEZH
Original site: B4R9P1_PHEZH 
ID   B4R9P1_PHEZH            Unreviewed;       160 AA.
AC   B4R9P1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524};
DE            Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN   Name=ssb {ECO:0000313|EMBL:ACG77805.1};
GN   OrderedLocusNames=PHZ_c1391 {ECO:0000313|EMBL:ACG77805.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77805.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG77805.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG77805.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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:0000256|HAMAP-Rule:MF_00984}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00984}.
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DR   EMBL; CP000747; ACG77805.1; -; Genomic_DNA.
DR   RefSeq; WP_012521949.1; NC_011144.1.
DR   AlphaFoldDB; B4R9P1; -.
DR   STRING; 450851.PHZ_c1391; -.
DR   KEGG; pzu:PHZ_c1391; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_1_5; -.
DR   OrthoDB; 9809878at2; -.
DR   Proteomes; UP000001868; 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; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00621; ssb; 1.
DR   PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR10302:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   Pfam; PF00436; SSB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00984}; DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00984};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT   DNA_BIND        54..60
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   REGION          115..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           155..160
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
SQ   SEQUENCE   160 AA;  17544 MW;  8A282DECA2E286AE CRC64;
     MAGSVNKVIL VGNLGADPEI RSLNSGDRVA NLRIATSETW RDRSTGERKE KTEWHRVVIF
     NENLVKVAEN YLRKGSTVYI EGSLQTRKWT DQSGQEKYST EIVLQKFRGE LTMLGGRGEG
     GGAADRDEGG YGGGFSSGPR AQSSGPREDF SADLDDEIPF
//
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