ID L0WI13_9GAMM Unreviewed; 498 AA.
AC L0WI13;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EKF75797.1};
GN ORFNames=A11A3_02972 {ECO:0000313|EMBL:EKF75797.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF75797.1, ECO:0000313|Proteomes:UP000010164};
RN [1] {ECO:0000313|EMBL:EKF75797.1, ECO:0000313|Proteomes:UP000010164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF75797.1,
RC ECO:0000313|Proteomes:UP000010164};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(2012).
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:EKF75797.1}.
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DR EMBL; AMRJ01000002; EKF75797.1; -; Genomic_DNA.
DR RefSeq; WP_008927781.1; NZ_AMRJ01000002.1.
DR AlphaFoldDB; L0WI13; -.
DR STRING; 1177179.A11A3_02972; -.
DR MEROPS; S13.003; -.
DR PATRIC; fig|1177179.3.peg.593; -.
DR eggNOG; COG2027; Bacteria.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000010164; 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; 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:EKF75797.1};
KW Hydrolase {ECO:0000313|EMBL:EKF75797.1};
KW Protease {ECO:0000313|EMBL:EKF75797.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003948008"
SQ SEQUENCE 498 AA; 55118 MW; C1895F099D2D870B CRC64;
MLYCATRWLT VALLLFAGPA MAEPVAADLP HPQLQPVLNQ AQKIDLPDQA LALAAIPLNG
PGKARYVNPD EAVSPGSIMK LVTTYAALEL LGPNYHWHTR LYTDGTIDGD TLNGNLYFVG
SGDPKLTEER LWQLLRELRG YGIRTINGQL RLDGSFFHLP NGIHDFNDDG DNPNAPFLVE
PDSLLTNLNV VRLRARADDR GIHTWMEPDL ASVTVNNQLV FKTFGHCPAR YQYDFQPRTL
SNGKVEVTVT GVLPRDCSTD SYLSLFSQRD YTAALLTSLW QQVGGTFTDK ADIDHTHLAT
LPRGATLLAT TSSRDLVTMV RDINKWSNNV MARQLFLTIG AERRQPDDQD DLAAAEREIR
QWLAHKGIDG HAMVFENGAG LSRIERITAG QMAQLLEQAW HSPYSAELIS SLPLAAMDGT
MRRRLRDADM DGLAHIKTGS LNNVRSVAGF ARDDNNTTWA VVAVINHQQA WKTEAVLDTL
LKQIHLAARP TTITTATN
//
