RSPB_ECOLI
ID RSPB_ECOLI Reviewed; 339 AA.
AC P38105;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Starvation-sensing protein RspB;
DE EC=1.1.1.-;
GN Name=rspB {ECO:0000303|PubMed:7545940}; OrderedLocusNames=b1580, JW1572;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7545940; DOI=10.1126/science.7545940;
RA Huisman G.W., Kolter R.;
RT "Sensing starvation: a homoserine lactone-dependent signaling pathway in
RT Escherichia coli.";
RL Science 265:537-539(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22972332; DOI=10.1271/bbb.120273;
RA Sakihama Y., Mizoguchi H., Oshima T., Ogasawara N.;
RT "YdfH identified as a repressor of rspA by the use of reduced genome
RT Escherichia coli MGF-01.";
RL Biosci. Biotechnol. Biochem. 76:1688-1693(2012).
CC -!- FUNCTION: Not known; probable catabolic enzyme.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- INDUCTION: Repressed by RspR. {ECO:0000269|PubMed:22972332}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L31628; AAA21686.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74652.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15284.1; -; Genomic_DNA.
DR PIR; I81185; I81185.
DR RefSeq; NP_416097.1; NC_000913.3.
DR RefSeq; WP_000836066.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P38105; -.
DR SMR; P38105; -.
DR BioGRID; 4260232; 14.
DR BioGRID; 850487; 1.
DR IntAct; P38105; 1.
DR STRING; 511145.b1580; -.
DR PaxDb; P38105; -.
DR PRIDE; P38105; -.
DR EnsemblBacteria; AAC74652; AAC74652; b1580.
DR EnsemblBacteria; BAA15284; BAA15284; BAA15284.
DR GeneID; 946127; -.
DR KEGG; ecj:JW1572; -.
DR KEGG; eco:b1580; -.
DR PATRIC; fig|1411691.4.peg.682; -.
DR EchoBASE; EB2346; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR InParanoid; P38105; -.
DR OMA; PIGCLHV; -.
DR PhylomeDB; P38105; -.
DR BioCyc; EcoCyc:G6838-MON; -.
DR PRO; PR:P38105; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008868; F:galactitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..339
FT /note="Starvation-sensing protein RspB"
FT /id="PRO_0000160900"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 36564 MW; E0A1062DFB7C114E CRC64;
MKSILIEKPN QLAIVEREIP TPSAGEVRVK VKLAGICGSD SHIYRGHNPF AKYPRVIGHE
FFGVIDAVGE GVESARVGER VAVDPVVSCG HCYPCSIGKP NVCTTLAVLG VHADGGFSEY
AVVPAKNAWK IPEAVADQYA VMIEPFTIAA NVTGHGQPTE NDTVLVYGAG PIGLTIVQVL
KGVYNVKNVI VADRIDERLE KAKESGADWA INNSQTPLGE IFTEKGIKPT LIIDAACHPS
ILKEAVTLAS PAARIVLMGF SSEPSEVIQQ GITGKELSIF SSRLNANKFP IVIDWLSKGL
IKPEKLITHT FDFQHVADAI SLFEQDQKHC CKVLLTFSE
