ID A0A0H3GSR8_KLEPH Unreviewed; 316 AA.
AC A0A0H3GSR8;
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=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:AEW62333.1};
GN OrderedLocusNames=KPHS_36350 {ECO:0000313|EMBL:AEW62333.1};
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:AEW62333.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW62333.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW62333.1,
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 S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP003200; AEW62333.1; -; Genomic_DNA.
DR RefSeq; WP_004180615.1; NC_016845.1.
DR RefSeq; YP_005227935.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GSR8; -.
DR STRING; 1125630.KPHS_36350; -.
DR GeneID; 11848666; -.
DR KEGG; kpm:KPHS_36350; -.
DR PATRIC; fig|1125630.4.peg.3542; -.
DR HOGENOM; CLU_027070_0_3_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..316
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002610303"
FT DOMAIN 31..262
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 316 AA; 34684 MW; 7EB792574734B887 CRC64;
MMPKFRVSLL SLTLLLAVPF APQALAKTPT AVTASQPEIA SGSAMIVDLA TKKIIYASQP
DLVRPMASIT KVMTAMVVLD AHLPLDEMLT VDISHTPEMK GIYSRVRLNS QISRRDMLLL
ALMSSENRAA ASLAHHYPGG YDAFIRAMNA KAQALGMTHT RYVEPTGLSV HNVSTARDLT
KLLIASEQYP LIGQLSTTKE ETATFAHPAY SLPFRNTNHL VYRDNWNIQL TKTGFTNAAG
HCLIMRTVIN QRPVALVVMD AFGKYTHFAD ASRLRTWIET GKVMPVPASA LSYKKQREAQ
MAEAMLKGGA QTAQND
//
