ID I0WHQ1_9FLAO Unreviewed; 296 AA.
AC I0WHQ1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Peptidase U61, LD-carboxypeptidase A {ECO:0000313|EMBL:EID75917.1};
GN ORFNames=W5A_03204 {ECO:0000313|EMBL:EID75917.1};
OS Imtechella halotolerans K1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Imtechella.
OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID75917.1, ECO:0000313|Proteomes:UP000005938};
RN [1] {ECO:0000313|EMBL:EID75917.1, ECO:0000313|Proteomes:UP000005938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1 {ECO:0000313|EMBL:EID75917.1,
RC ECO:0000313|Proteomes:UP000005938};
RX PubMed=22740661; DOI=10.1128/JB.00506-12;
RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.;
RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans
RT K1T.";
RL J. Bacteriol. 194:3731-3731(2012).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:EID75917.1}.
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; AJJU01000003; EID75917.1; -; Genomic_DNA.
DR RefSeq; WP_008237354.1; NZ_AJJU01000003.1.
DR AlphaFoldDB; I0WHQ1; -.
DR STRING; 946077.W5A_03204; -.
DR PATRIC; fig|946077.3.peg.648; -.
DR eggNOG; COG1619; Bacteria.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000005938; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:EID75917.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005938};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 169..285
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 296 AA; 32946 MW; 29CB0A0AAC06C492 CRC64;
MLLPKPLQPG DTVAIVATAR KIDEEELTAA VALLESWGLK VLIGNSIGLQ DRQFAGTDSE
RFADFQTMLY NPTVKGIWCA RGGYGTVRII DILNFSDFSN HPKWIVGYSD ITVLHSHLNT
LRIASMHATM PVNISRNSAA SLASLKTALF GQKNVYDFPH ESKKLDTITG ELVGGNLSIL
YSLLGSSSSI DTRGKILFLE DLDEYLYHVD RMMMNLKRNG YFDEIKALLV GGMTKMKDNS
IPFGKTAREI IEDVCKNFDF PIIFDVPAGH IQDNRTLIIG KEITIKIGYD KVQLIQ
//