ID A0A0H3GTZ2_KLEPH Unreviewed; 345 AA.
AC A0A0H3GTZ2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:AEW61747.1};
GN OrderedLocusNames=KPHS_30490 {ECO:0000313|EMBL:AEW61747.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW61747.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW61747.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW61747.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP003200; AEW61747.1; -; Genomic_DNA.
DR RefSeq; WP_004200181.1; NC_016845.1.
DR RefSeq; YP_005227349.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GTZ2; -.
DR STRING; 1125630.KPHS_30490; -.
DR GeneID; 11848070; -.
DR KEGG; kpm:KPHS_30490; -.
DR PATRIC; fig|1125630.4.peg.2970; -.
DR HOGENOM; CLU_034346_1_1_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 15..135
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 209..332
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 345 AA; 37856 MW; 1B720CB9F4151539 CRC64;
MSVLFPPRLA PGDVIGVTAP SAGVPEHLHP RLELAIKNLK KRGYQVREGR CLRSQHKNKS
ATKFSRVEEL MSYLTDPDIK AVMPPWGGDL AMELLDLIDF DLLSRSKPKW FVGFSDLSTL
HFPLTTISGW ATLHGPNLMD LGAQKLDATT QAVWEILESN RGTVIKQYSS TAFQADENQW
GTASDGGFNL TQKTQWKRLD GVTSSLTFSG KLIGGCLEII SRLAGTPFGN VPLFKASNSP
QGIILYFENV EMAPCELTRA LFSLRLQGWF DNLNGVLIGR SAAPDVSDPT KHNYLDALKA
AFENIAVPVL YDVDIGHIPP QISLVNGADA TVFFAENGSW VTQQL
//
