ID   A0A1C6LLK3_9NEIS        Unreviewed;       464 AA.
AC   A0A1C6LLK3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SCK07382.1};
GN   ORFNames=PSELUDRAFT_0367 {ECO:0000313|EMBL:SCK07382.1};
OS   Vogesella sp. LIG4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK07382.1, ECO:0000313|Proteomes:UP000198213};
RN   [1] {ECO:0000313|EMBL:SCK07382.1, ECO:0000313|Proteomes:UP000198213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607802; SCK07382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6LLK3; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000198213; Chromosome i.
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:SCK07382.1};
KW   Hydrolase {ECO:0000313|EMBL:SCK07382.1};
KW   Protease {ECO:0000313|EMBL:SCK07382.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198213};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008739729"
SQ   SEQUENCE   464 AA;  49243 MW;  17EAAA69404E674D CRC64;
     MKRLLLLLAV VAAPLYAAAP AGFNDDEIAL WAAPVEGGVF EAHRAEQAVN PASTMKLLTS
     WAALNRLGPN FRWQTEFRSS APLQNGVLQG DLYWLGRGDP RLDSARLTEM LRQLRLRGVR
     DIAGRLVLDQ SAWQGLGAAD GFGGDADRVF TVAPHTHQLN LKVAWLRYYF DNGQPQALLD
     PPLPGVSVDS RLQAAAGNGS SCGDVRRYVK VVQQGARLGV SGSLPPACDG AANYVNLLDS
     NEFAQQAFAA LWQQLGGSGP RGLALATTPA GARSLLRQDS ADTLAGVLVD MNKYSNNTMA
     RSVLLTLGAQ YPASGNTFAD GERQLRSLLV EHALPQQPLL LENGAGLSRR ERVSAQLLGE
     VLRDALRGPY GPELAASLPL AGEDGTLKKR LGDVGGSLRL KTGSLDNVRA LAGYWQAPSG
     QRLVLVAIVN SPRADKLTPQ LDAAVAALVA RYQARLAASA AAGL
//