ID   A0A1G9TPG5_9ACTN        Unreviewed;       472 AA.
AC   A0A1G9TPG5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SDM49551.1};
GN   ORFNames=SAMN05660642_02588 {ECO:0000313|EMBL:SDM49551.1};
OS   Geodermatophilus siccatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1137991 {ECO:0000313|EMBL:SDM49551.1, ECO:0000313|Proteomes:UP000198680};
RN   [1] {ECO:0000313|EMBL:SDM49551.1, ECO:0000313|Proteomes:UP000198680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45419 {ECO:0000313|EMBL:SDM49551.1,
RC   ECO:0000313|Proteomes:UP000198680};
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}.
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DR   EMBL; FNHE01000006; SDM49551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9TPG5; -.
DR   STRING; 1137991.SAMN05660642_02588; -.
DR   OrthoDB; 56883at2; -.
DR   Proteomes; UP000198680; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDM49551.1};
KW   Hydrolase {ECO:0000313|EMBL:SDM49551.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDM49551.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   472 AA;  45709 MW;  640B5BDB618ED054 CRC64;
     MGTIAGSGSA TVTPKYSRFR RRLLLGVLVL VLAVAAGVWF VLAPRGDGAA TEVAAPEARL
     PDVEPAAPVL AALPSQAPTP DATVLAGELT PLLGSPALGA GVEAQVVDVA SGEVLFDQDG
     DSPSTPASTA KLLTAVAALT TLGPDATLET TVVAGATPGE VVLVGGGDPT LSRTVPSLTY
     PGAATVADLA AQVRSGLPVG TQVTRVVVDN SLFEGPLTAG GWGPGDAPST YAAPVTATAV
     DGARVSPSEQ QRSAAPGTDA GTALAVALGA PGATVVLGDA PQGAPTLGTV RSAPVARLVE
     QALSQSDNLL TESLARHVAL AGGRPATFDG AAEAVTDALS GLGLDVTGLS LADGSGLSAT
     DRVPVALLAD LLTGAADGTL ADASAVLSGL PVAGYDGTLA ERGDDDPGTA PGSVRAKTGT
     LLGVHGLAGT VVTAEGRLLV FAVLADGAPA NGLAAEAALD DVASALAACG CR
//