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Single-stranded DNA-binding protein (Gp32) (Helix-destabilizing protein)

 VHED_BPT4               Reviewed;         301 AA.
P03695; Q38555;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 109.
RecName: Full=Single-stranded DNA-binding protein;
AltName: Full=Gp32;
AltName: Full=Helix-destabilizing protein;
Name=32; Synonyms=ssb;
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMBER MUTANT 32AMA453).
PubMed=6289325; DOI=10.1073/pnas.79.16.4937;
Krisch H.M., Allet B.;
"Nucleotide sequences involved in bacteriophage T4 gene 32
translational self-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 79:4937-4941(1982).
[2]
PROTEIN SEQUENCE.
PubMed=6257686;
Williams K.R., Lopresti M.B., Setoguchi M.;
"Primary structure of the bacteriophage T4 DNA helix-destabilizing
protein.";
J. Biol. Chem. 256:1754-1762(1981).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[4]
PRELIMINARY PROTEIN SEQUENCE OF 1-74 AND 94-282.
PubMed=6997174;
Pan Y.-C.E., Nakashima Y., Sharief F.S., Li S.S.-L.;
"Amino acid sequence studies on T4 gene 32 DNA-binding proteins.";
Hoppe-Seyler's Z. Physiol. Chem. 361:1139-1153(1980).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-301 (MUTANT DELTA PR201).
PubMed=8429554; DOI=10.1006/jmbi.1993.1042;
Hurley J.M., Chervitz S.A., Jarvis T.C., Singer B.S., Gold L.;
"Assembly of the bacteriophage T4 replication machine requires the
acidic carboxy terminus of gene 32 protein.";
J. Mol. Biol. 229:398-418(1993).
[6]
ZINC-LIGANDS.
PubMed=1731933; DOI=10.1021/bi00118a018;
Giedroc D.P., Qiu H., Khan R., King G.C., Chen K.;
"Zn(II) coordination domain mutants of T4 gene 32 protein.";
Biochemistry 31:765-774(1992).
[7]
DOMAIN LAST.
PubMed=1736285; DOI=10.1073/pnas.89.3.1050;
Casas-Finet J.R., Fischer K.R., Karpel R.L.;
"Structural basis for the nucleic acid binding cooperativity of
bacteriophage T4 gene 32 protein: the (Lys/Arg)3(Ser/Thr)2 (LAST)
motif.";
Proc. Natl. Acad. Sci. U.S.A. 89:1050-1054(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-239.
PubMed=7630406; DOI=10.1038/376362a0;
Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A.;
"Crystal structure of a replication fork single-stranded DNA binding
protein (T4 gp32) complexed to DNA.";
Nature 376:362-366(1995).
[9]
ERRATUM.
Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A.;
Nature 376:616-616(1995).
-!- FUNCTION: Binds preferentially to single-stranded DNA and
therefore, destabilizes double-stranded DNA. It is involved in DNA
replication, repair and recombination. Binds ss-DNA as the
replication fork advances and stimulates the replisome
processivity and accuracy.
-!- SUBUNIT: Homodimer in the absence of DNA, monomer when binding
DNA.
-!- DOMAIN: The (Lys/Arg)3(Ser/Thr)2 (LAST) motif is involved in the
cooperative binding of the protein to single-stranded nucleic
acids. {ECO:0000269|PubMed:1736285}.
-!- MISCELLANEOUS: Interacts with the polymerase and the uvsX and uvsY
proteins. Binds tightly to dDA protein.
-----------------------------------------------------------------------
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EMBL; J02513; AAA32511.1; -; Genomic_DNA.
EMBL; AF158101; AAD42454.1; -; Genomic_DNA.
EMBL; S54962; AAB25300.1; -; Genomic_DNA.
PIR; A93924; DDBP34.
RefSeq; NP_049854.1; NC_000866.4.
PDB; 1GPC; X-ray; 2.20 A; A=22-239.
PDB; 1WAI; Model; -; S=22-239.
PDBsum; 1GPC; -.
PDBsum; 1WAI; -.
ProteinModelPortal; P03695; -.
SMR; P03695; -.
GeneID; 1258602; -.
KEGG; vg:1258602; -.
KO; K18946; -.
OrthoDB; VOG090000JW; -.
EvolutionaryTrace; P03695; -.
Proteomes; UP000009087; Genome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR012339; Phage_T4_Gp32_ssDNA-bd.
Pfam; PF08804; gp32; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA recombination; DNA repair; DNA replication;
DNA-binding; Metal-binding; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 301 Single-stranded DNA-binding protein.
/FTId=PRO_0000165047.
REGION 3 8 LAST.
METAL 64 64 Zinc.
METAL 77 77 Zinc.
METAL 87 87 Zinc.
METAL 90 90 Zinc.
VARIANT 116 301 Missing (in mutant 32AMA453).
VARIANT 292 296 Missing (in mutant delta PR201).
CONFLICT 86 86 S -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 91 91 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 124 124 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 156 156 E -> Q (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 194 194 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 202 202 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 212 212 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 223 223 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 276 277 DD -> NN (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 26 28 {ECO:0000244|PDB:1GPC}.
STRAND 41 47 {ECO:0000244|PDB:1GPC}.
STRAND 51 55 {ECO:0000244|PDB:1GPC}.
STRAND 57 68 {ECO:0000244|PDB:1GPC}.
STRAND 71 76 {ECO:0000244|PDB:1GPC}.
HELIX 78 81 {ECO:0000244|PDB:1GPC}.
HELIX 88 95 {ECO:0000244|PDB:1GPC}.
HELIX 98 101 {ECO:0000244|PDB:1GPC}.
HELIX 103 109 {ECO:0000244|PDB:1GPC}.
STRAND 112 123 {ECO:0000244|PDB:1GPC}.
HELIX 128 130 {ECO:0000244|PDB:1GPC}.
STRAND 134 139 {ECO:0000244|PDB:1GPC}.
HELIX 141 148 {ECO:0000244|PDB:1GPC}.
TURN 149 151 {ECO:0000244|PDB:1GPC}.
HELIX 155 157 {ECO:0000244|PDB:1GPC}.
TURN 167 169 {ECO:0000244|PDB:1GPC}.
STRAND 173 180 {ECO:0000244|PDB:1GPC}.
STRAND 183 185 {ECO:0000244|PDB:1GPC}.
TURN 198 201 {ECO:0000244|PDB:1GPC}.
HELIX 203 212 {ECO:0000244|PDB:1GPC}.
HELIX 216 220 {ECO:0000244|PDB:1GPC}.
HELIX 228 238 {ECO:0000244|PDB:1GPC}.
SEQUENCE 301 AA; 33506 MW; 4C9771CF5D978487 CRC64;
MFKRKSTAEL AAQMAKLNGN KGFSSEDKGE WKLKLDNAGN GQAVIRFLPS KNDEQAPFAI
LVNHGFKKNG KWYIETCSST HGDYDSCPVC QYISKNDLYN TDNKEYSLVK RKTSYWANIL
VVKDPAAPEN EGKVFKYRFG KKIWDKINAM IAVDVEMGET PVDVTCPWEG ANFVLKVKQV
SGFSNYDESK FLNQSAIPNI DDESFQKELF EQMVDLSEMT SKDKFKSFEE LNTKFGQVMG
TAVMGGAAAT AAKKADKVAD DLDAFNVDDF NTKTEDDFMS SSSGSSSSAD DTDLDDLLND
L


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