SSB_PSEAE
ID SSB_PSEAE Reviewed; 165 AA.
AC P40947;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
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=PA4232;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-38 AND 52-63, AND
RP SUBUNIT.
RC STRAIN=PAO / DSM 1707;
RX PubMed=8982079; DOI=10.1016/s0378-1119(96)00535-5;
RA Genschel J., Litz L., Thole H., Roemling U., Urbanke C.;
RT "Isolation, sequencing and overproduction of the single-stranded DNA
RT binding protein from Pseudomonas aeruginosa PAO.";
RL Gene 182:137-143(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 ECO:0000269|PubMed:8982079}.
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DR EMBL; Z32859; CAA83688.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07620.1; -; Genomic_DNA.
DR PIR; JC5485; S44302.
DR RefSeq; NP_252922.1; NC_002516.2.
DR RefSeq; WP_003114685.1; NZ_QZGE01000028.1.
DR PDB; 5YUN; X-ray; 2.67 A; A/B/C/D=1-115.
DR PDB; 5YUO; X-ray; 2.04 A; A/B/C/D=1-115.
DR PDB; 6IRQ; X-ray; 1.91 A; A/B/C/D=1-115.
DR PDB; 6JDG; X-ray; 2.39 A; A/B/C/D=1-115.
DR PDB; 7VUM; X-ray; 2.32 A; A/B/C/D=1-115.
DR PDBsum; 5YUN; -.
DR PDBsum; 5YUO; -.
DR PDBsum; 6IRQ; -.
DR PDBsum; 6JDG; -.
DR PDBsum; 7VUM; -.
DR AlphaFoldDB; P40947; -.
DR SMR; P40947; -.
DR STRING; 287.DR97_3679; -.
DR PaxDb; P40947; -.
DR PRIDE; P40947; -.
DR EnsemblBacteria; AAG07620; AAG07620; PA4232.
DR GeneID; 881822; -.
DR KEGG; pae:PA4232; -.
DR PATRIC; fig|208964.12.peg.4433; -.
DR PseudoCAP; PA4232; -.
DR HOGENOM; CLU_078758_0_2_6; -.
DR InParanoid; P40947; -.
DR OMA; GQMQERT; -.
DR PhylomeDB; P40947; -.
DR BioCyc; PAER208964:G1FZ6-4305-MON; -.
DR Proteomes; UP000002438; 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; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; DNA replication; DNA-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8982079"
FT CHAIN 2..165
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096078"
FT DOMAIN 5..110
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 109..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..165
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:6IRQ"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 76..89
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:6IRQ"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6IRQ"
SQ SEQUENCE 165 AA; 18557 MW; 48FF2A38FD74E551 CRC64;
MARGVNKVIL VGNVGGDPET RYMPNGNAVT NITLATSESW KDKQTGQQQE RTEWHRVVFF
GRLAEIAGEY LRKGSQVYVE GSLRTRKWQG QDGQDRYTTE IVVDINGNMQ LLGGRPSGDD
SQRAPREPMQ RPQQAPQQQS RPAPQQQPAP QPAQDYDSFD DDIPF
