ID   YFEW_ECO57              Reviewed;         434 AA.
AC   Q8XBJ0;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_01034};
DE   AltName: Full=DD-carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034};
DE            Short=DD-CPase {ECO:0000255|HAMAP-Rule:MF_01034};
GN   Name=yfeW {ECO:0000255|HAMAP-Rule:MF_01034};
GN   OrderedLocusNames=Z3695, ECs3301;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01034}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01034}.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family. YfeW subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01034}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG57548.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG57548.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB36724.1; -; Genomic_DNA.
DR   PIR; E91041; E91041.
DR   PIR; H85885; H85885.
DR   RefSeq; NP_311328.1; NC_002695.1.
DR   RefSeq; WP_001302015.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XBJ0; -.
DR   SMR; Q8XBJ0; -.
DR   STRING; 155864.EDL933_3593; -.
DR   MEROPS; S12.A03; -.
DR   EnsemblBacteria; AAG57548; AAG57548; Z3695.
DR   EnsemblBacteria; BAB36724; BAB36724; ECs_3301.
DR   GeneID; 915366; -.
DR   KEGG; ece:Z3695; -.
DR   KEGG; ecs:ECs_3301; -.
DR   PATRIC; fig|386585.9.peg.3448; -.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_020027_1_2_6; -.
DR   OMA; AGWAVRY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
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_0000036257"
FT   TRANSMEM        7..25
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ   SEQUENCE   434 AA;  47550 MW;  999F364BCB193292 CRC64;
     MKRTMLYLSL LAVSCSVSAA KYPVLTESSP EKAGFNVERL NQMDRWISQQ VDAGYPGVNL
     LIIKDNQIVY RKAWGAAKKY DGSVLMAQPV KATTGTLYDL ASNTKMYATN FALQKLMSEG
     KLHPDDLIAK YISGFADSPN DTIKGKNTLR ISDLLHHSGG FPADPQYPNK AVAGALYSQD
     KGQTLEMIKR TPLEYQPGSK HIYSDVDYML LGFIVESVTG QPLDRYVEES IYRPLGLTHT
     VFNPLLKGFK PQQIAATELN GNTRDGVIHF PNIRTSTHWG QVHDEKAFYS MGGVSGHAGL
     FSNTGDIAVL MQTMLNGGGY GDVQLFSAET VKMFTTSSKE DATFGLGWRV NGNATMTPTF
     GTLASPQTYG HTGWTGTVTV IDPVNHMAIV MLSNKPHSPV ADPQKNPNMF ESGQLPIATY
     GWVVDQVYAA LKQK