YFEW_ECOLI
ID YFEW_ECOLI Reviewed; 434 AA.
AC P77619;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000305};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000269|PubMed:16402224};
DE AltName: Full=DD-carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000303|PubMed:16402224};
DE Short=DD-CPase {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000303|PubMed:16402224};
DE AltName: Full=Penicillin binding protein 4B {ECO:0000305};
GN Name=yfeW {ECO:0000255|HAMAP-Rule:MF_01034};
GN Synonyms=pbp4B {ECO:0000303|PubMed:16402224};
GN OrderedLocusNames=b2430, JW5395;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16402224; DOI=10.1007/s00203-005-0057-5;
RA Vega D., Ayala J.A.;
RT "The DD-carboxypeptidase activity encoded by pbp4B is not essential for the
RT cell growth of Escherichia coli.";
RL Arch. Microbiol. 185:23-27(2006).
CC -!- FUNCTION: Penicillin-binding protein. Has low DD-carboxypeptidase
CC activity. {ECO:0000269|PubMed:16402224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01034, ECO:0000269|PubMed:16402224};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01034, ECO:0000305|PubMed:16402224}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000305|PubMed:16402224}.
CC -!- DISRUPTION PHENOTYPE: Not essential for cell growth.
CC {ECO:0000269|PubMed:16402224}.
CC -!- SIMILARITY: Belongs to the peptidase S12 family. YfeW subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01034, ECO:0000305}.
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DR EMBL; U00096; AAC75483.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16314.2; -; Genomic_DNA.
DR PIR; E65017; E65017.
DR RefSeq; NP_416925.2; NC_000913.3.
DR RefSeq; WP_001327042.1; NZ_LN832404.1.
DR AlphaFoldDB; P77619; -.
DR SMR; P77619; -.
DR BioGRID; 4260747; 340.
DR DIP; DIP-12021N; -.
DR STRING; 511145.b2430; -.
DR MEROPS; S12.A03; -.
DR jPOST; P77619; -.
DR PaxDb; P77619; -.
DR PRIDE; P77619; -.
DR EnsemblBacteria; AAC75483; AAC75483; b2430.
DR EnsemblBacteria; BAA16314; BAA16314; BAA16314.
DR GeneID; 946907; -.
DR KEGG; ecj:JW5395; -.
DR KEGG; eco:b2430; -.
DR PATRIC; fig|1411691.4.peg.4301; -.
DR EchoBASE; EB3916; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_1_2_6; -.
DR InParanoid; P77619; -.
DR OMA; AGWAVRY; -.
DR PhylomeDB; P77619; -.
DR BioCyc; EcoCyc:G7265-MON; -.
DR BioCyc; MetaCyc:G7265-MON; -.
DR PRO; PR:P77619; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_01034; S12_YfeW; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR022849; Pept_S12_YfeW/YbbE-like.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Putative D-alanyl-D-alanine carboxypeptidase"
FT /id="PRO_0000036256"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01034,
FT ECO:0000305|PubMed:16402224"
SQ SEQUENCE 434 AA; 47752 MW; 9CA0FDA5347A5468 CRC64;
MKRTMLYLSL LAVSCSVSAA KYPVLTESSP EKAGFNVERL NQMDRWISQQ VDVGYPSVNL
LIIKDNQIVY RKAWGAAKKY DGSVLMEQPV KATTGTLYDL ASNTKMYATN FALQKLMSEG
KLHPDDRIAK YIPGFADSPN DTIKGKNTLR ISDLLHHSGG FPADPQYPNK AVAGALYSQD
KGQTLEMIKR TPLEYQPGSK HIYSDVDYML LGFIVESVTG QPLDRYVEES IYRPLGLTHT
VFNPLLKGFK PQQIAATELN GNTRDGVIHF PNIRTSTLWG QVHDEKAFYS MGGVSGHAGL
FSNTGDIAVL MQTMLNGGGY GDVQLFNAET VKMFTTSSKE DATFGLGWRV NGNATMTPTF
GTLASPQTYG HTGWTGTVTV IDPVNHMTIV MLSNKPHSPV ADPQKNPNMF ESGQLPIATY
GWVVDQVYAA LKQK
