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Database: UniProt
Entry: I0WHQ1_9FLAO
LinkDB: I0WHQ1_9FLAO
Original site: I0WHQ1_9FLAO 
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}.
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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
//
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