ID   A0A1H3W5Z7_9GAMM        Unreviewed;       510 AA.
AC   A0A1H3W5Z7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family {ECO:0000313|EMBL:SDZ82513.1};
GN   ORFNames=SAMN05660964_00312 {ECO:0000313|EMBL:SDZ82513.1};
OS   Thiothrix caldifontis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=525918 {ECO:0000313|EMBL:SDZ82513.1, ECO:0000313|Proteomes:UP000199397};
RN   [1] {ECO:0000313|EMBL:SDZ82513.1, ECO:0000313|Proteomes:UP000199397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21228 {ECO:0000313|EMBL:SDZ82513.1,
RC   ECO:0000313|Proteomes:UP000199397};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNQP01000002; SDZ82513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3W5Z7; -.
DR   STRING; 525918.SAMN05660964_00312; -.
DR   Proteomes; UP000199397; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDZ82513.1};
KW   Hydrolase {ECO:0000313|EMBL:SDZ82513.1};
KW   Protease {ECO:0000313|EMBL:SDZ82513.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..510
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011462070"
FT   REGION          72..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  54897 MW;  D715D0EC83F5CCD4 CRC64;
     MKNGESMRIL HLGTLLMLSV SLVACSSQNV QPGTAVASAG TTHTQAELFG ETPSQTSVPQ
     AATPVQQSQW QARTANHQAS AEPVAKLQPT PLNSAGGDKT YRGAGKLNRL PDNIASSLRL
     RGLSEQNLGA YVRPVNGGQP LLVAYADTPR NPASTMKLVT SYAALGVLGP DYRWPTEIYT
     IGNVAGDTLQ GDVIIKGYGN PDFREADFRQ LLQALRARGI RNIAGNFVVD KTYFNVPYQA
     AIDGKEGASY NAQPEALLYN ERGSCYEMRN KAGQIQRICP IAPRNGNDLN VNLFGDFWKI
     WVGEMGGHLN GGLQVQAVPA GAQLVSTHQS APLRDVLVEI NKDSNNVKAR QVLLSMGAKQ
     FGAPGTTQKG AGAVGQFMES RGLRFSNLKI ENGSGLSRVE RISTREMGEM LVDAYNSPYR
     DELMRSMAVL GVDGTVKSRL KNLAGRGKFK TGTLRDVRAL AGYLTAANGQ TYVVALLHND
     ASIRATAKES HDDLVEWVYY GAQNNVASAQ
//