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Database: UniProt
Entry: A0A177QH39_9GAMM
LinkDB: A0A177QH39_9GAMM
Original site: A0A177QH39_9GAMM 
ID   A0A177QH39_9GAMM        Unreviewed;       457 AA.
AC   A0A177QH39;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYO45_06295 {ECO:0000313|EMBL:OAI46564.1};
OS   Gammaproteobacteria bacterium SCGC AG-212-F23.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1799661 {ECO:0000313|EMBL:OAI46564.1, ECO:0000313|Proteomes:UP000092275};
RN   [1] {ECO:0000313|Proteomes:UP000092275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-F23 {ECO:0000313|Proteomes:UP000092275};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAI46564.1}.
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DR   EMBL; LSTE01000103; OAI46564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QH39; -.
DR   Proteomes; UP000092275; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 2.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000092275};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..457
FT                   /note="D-alanyl-D-alanine carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008071415"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  49239 MW;  D94179DE36EB0DC0 CRC64;
     MALLKKCLLG IVFVGMAASG NTQVLAKHHH HHTHHSTHHY SPPVEDVAPL PSAVNGKSNL
     SDAINTIIAG ADPEASIGIV VKSMKSGDIL YEHNAKQLFV PASTMKILTA EAALLYLGPQ
     YKFPTSIFTD ARSINKGVID GNIYIVHSGD PSLTVYDIHD LMASLKAMQI QRITGNVYID
     TSAYDQQNFG PGWIGSDKRY CYGAPISASI INHNCLASSR GLLHTSKAKL KSVGSAVIND
     VIKFNQILMQ ESFKRLGISV HGNIKIGSTP PYASRLATHE SKQLHSLVST MLKKSDNIIA
     GSLFKKIGAL YTRQPGSWSN GSAAVKDILS KQAGVDASGA MILDGSGLSP ENTISPSQLM
     QVLTFAYHHS SSSYDFISAL PISGVDGTLK HRLTNISWKV RAKTGTMAGV RSLAGYAMTR
     DNEPLAFVIM VNGRNSAGYS YKEVEDRIVT VLTKYSQ
//
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