FRVX_ECOLI
ID FRVX_ECOLI Reviewed; 356 AA.
AC P32153; Q2M8J5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative aminopeptidase FrvX;
DE EC=3.4.11.-;
GN Name=frvX; Synonyms=yiiI; OrderedLocusNames=b3898, JW3869;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
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 [3]
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 [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8019415; DOI=10.1002/pro.5560030309;
RA Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis: unique, putative fructose- and glucoside-specific systems.";
RL Protein Sci. 3:440-450(1994).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR EMBL; L19201; AAB03031.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76880.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77411.1; -; Genomic_DNA.
DR PIR; S40842; S40842.
DR RefSeq; NP_418334.1; NC_000913.3.
DR RefSeq; WP_001019484.1; NZ_LN832404.1.
DR AlphaFoldDB; P32153; -.
DR SMR; P32153; -.
DR BioGRID; 4263328; 17.
DR DIP; DIP-9694N; -.
DR IntAct; P32153; 4.
DR STRING; 511145.b3898; -.
DR PaxDb; P32153; -.
DR PRIDE; P32153; -.
DR EnsemblBacteria; AAC76880; AAC76880; b3898.
DR EnsemblBacteria; BAE77411; BAE77411; BAE77411.
DR GeneID; 948388; -.
DR KEGG; ecj:JW3869; -.
DR KEGG; eco:b3898; -.
DR PATRIC; fig|1411691.4.peg.2809; -.
DR EchoBASE; EB1808; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_047249_0_2_6; -.
DR InParanoid; P32153; -.
DR OMA; FMAHMDE; -.
DR PhylomeDB; P32153; -.
DR BioCyc; EcoCyc:EG11862-MON; -.
DR PRO; PR:P32153; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; -; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..356
FT /note="Putative aminopeptidase FrvX"
FT /id="PRO_0000071655"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 38733 MW; 8F399EFDA3ADE353 CRC64;
MNIELLQQLC EASAVSGDEQ EVRDILINTL EPCVNEITFD GLGSFVARKG NKGPKVAVVG
HMDEVGFMVT HIDESGFLRF TTIGGWWNQS MLNHRVTIRT HKGVKIPGVI GSVAPHALTE
KQKQQPLSFD EMFIDIGANS REEVEKRGVE IGNFISPEAN FACWGEDKVV GKALDNRIGC
AMMAELLQTV NNPEITLYGV GSVEEEVGLR GAQTSAEHIK PDVVIVLDTA VAGDVPGIDN
IKYPLKLGQG PGLMLFDKRY FPNQKLVAAL KSCAAHNDLP LQFSTMKTGA TDGGRYNVMG
GGRPVVALCL PTRYLHANSG MISKADYEAL LTLIRGFLTT LTAEKVNAFS QFRQVD
