ID A0A0K6HQP9_9BURK Unreviewed; 481 AA.
AC A0A0K6HQP9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family {ECO:0000313|EMBL:CUA93377.1};
GN ORFNames=Ga0061069_101206 {ECO:0000313|EMBL:CUA93377.1};
OS Thiomonas bhubaneswarensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=339866 {ECO:0000313|EMBL:CUA93377.1, ECO:0000313|Proteomes:UP000183649};
RN [1] {ECO:0000313|Proteomes:UP000183649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18181 {ECO:0000313|Proteomes:UP000183649};
RA Varghese N.;
RL Submitted (AUG-2015) 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; CYHF01000001; CUA93377.1; -; Genomic_DNA.
DR RefSeq; WP_055449166.1; NZ_LIPV01000001.1.
DR AlphaFoldDB; A0A0K6HQP9; -.
DR STRING; 339866.GCA_001418255_00204; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000183649; 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; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CUA93377.1};
KW Hydrolase {ECO:0000313|EMBL:CUA93377.1};
KW Protease {ECO:0000313|EMBL:CUA93377.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005504704"
SQ SEQUENCE 481 AA; 50927 MW; 26701CE297024186 CRC64;
MQVSRRLFLA STLALAGAPL MARAQQAGLG TTGALPASVT QALASARIPL QSCAFMLQAL
DSPAPEIDFN GAALMNPASV LKLVTTYAAL RILGPAYVWK TPVYAVGPVR AGVLQGDLAF
VGSGDPHLMA DNLWSIALRL RDLGIRRIRG DVLIDRQAFD LPPHDPAAFD GDATAPYNVG
PDPFLVNFGV MRLGFVPDPA AQQVRVTVEP PLAGFDLHAA PRLTATACGN WKDKLGADWK
QPFAPRFAGG YAAACGPQTW NIAPEVSDNT YVQRLLAALF AQVGIEWKGQ VRTAPLPAGA
TELTVWESPA LAVLVRDINK YSNNVMAQQV FLTLALAAGA QRATWAGAQQ AVQQWLAAHG
LNMPGLVLDN GCGLSRIARI SAADLNALLR SAWQSPVMPE FVSSLPLAGE DGTLRRHFRD
PDTAGRIHAK TGTLDGVLSL AGYAQARSGQ RYTFAALVND PRAGGAWPAL EAFVGGFMQT
A
//
