ID A0A1H7SW74_9BURK Unreviewed; 353 AA.
AC A0A1H7SW74;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=D-alanyl-D-alanine endopeptidase (Penicillin-binding protein 7) {ECO:0000313|EMBL:SEL76539.1};
GN ORFNames=SAMN05216319_2653 {ECO:0000313|EMBL:SEL76539.1};
OS Duganella sp. CF402.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL76539.1, ECO:0000313|Proteomes:UP000198529};
RN [1] {ECO:0000313|Proteomes:UP000198529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; FOBG01000001; SEL76539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7SW74; -.
DR STRING; 1855289.SAMN05216319_2653; -.
DR Proteomes; UP000198529; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..353
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011628491"
FT DOMAIN 92..319
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 126
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 353 AA; 37740 MW; 9D9662EBBBE9221B CRC64;
MIKLALSALI SLMFASAAIA APATDASGAA PKKQQVKNKR QPVRVAAADA GERIVKRVIK
VNGKRKVVYQ RVLAAAPATP TMGDLAGLNR TSDPLDLKSN VALVLDQANS EVLFEKNSNI
ALPIASITKM MTGLVVVEAK LDMDEVLTVT EEDVDREKFS SSRLKVGTQM TRANMLHIAL
MSSENRAASA LGRNYPGGKP AFVEAMNAKA RELGMTDTHY VDSSGLSKMN VASARDLAKL
AMAAYQQPVL RQFSTDPKAV VETSNGRPMA FGTTNHLVAS PDWAIGLQKT GFINEAGRCL
LMQAVIEGRS VIMVFLDSKG KQSRTADAGR MRKWLEALKP AGLSGSTSYS TGM
//
