ID   A0A1H2N4E6_9PSED        Unreviewed;       517 AA.
AC   A0A1H2N4E6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SDV00419.1};
GN   ORFNames=SAMN05216202_2993 {ECO:0000313|EMBL:SDV00419.1};
OS   Pseudomonas mucidolens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=46679 {ECO:0000313|EMBL:SDV00419.1, ECO:0000313|Proteomes:UP000198600};
RN   [1] {ECO:0000313|Proteomes:UP000198600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 2223 {ECO:0000313|Proteomes:UP000198600};
RA   Varghese N., Submissions S.;
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; LT629802; SDV00419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2N4E6; -.
DR   STRING; 46679.SAMN05216202_2993; -.
DR   Proteomes; UP000198600; Chromosome i.
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; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
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:SDV00419.1};
KW   Hydrolase {ECO:0000313|EMBL:SDV00419.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDV00419.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   517 AA;  55914 MW;  78816B70A4E00119 CRC64;
     MGHNADTFMT NEGFSCIALA FFTLLSSRVL FFMIKSLRPL LLASFLLPLA FSVTAAPINT
     SLPPKVQESL KKAKLQNDAL SLVMIPLTGP GTPTVFNADV SVNPASTMKL VTTYAALEML
     GPNHQWKTEF YTDGTLSGGI LRGNLYLKGG GDPKLNMEKL WLLMRDLRAN GVQQVTGDLV
     LDRGFFIQPQ LPAFNDDGND ANKPFLVKPD ALLVNLKALR FVTRNDSGRV LVSVEPPIAS
     IHIDNQVKPT NTKQCTGDVR YNPVTAADGS VTVTVSGQLG DGCSSQTYLS LLDHATYAAG
     AVRAIWKELG GSIQGRDVLA PVPKSAKLLA RAFSPDLAEI IRDINKYSNN TMAQQLFLSL
     GAQYRTDADG DDGKAAQRVI RQWLAKKGIT APHLVMENGS GLSRAERVSA RELARMLQAA
     WKSPYAAEFV SSMPIAGSDG TMRRRLKTTA LRGEAHIKTG TLNTVRAIAG YSRDNNGNTW
     AVVAILNDPK PWGASSVLDQ VLLDLYRQPK VTTASAL
//