ID A0A0Q4MW90_9GAMM Unreviewed; 533 AA.
AC A0A0Q4MW90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=ASF13_06205 {ECO:0000313|EMBL:KQN56710.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN56710.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN56710.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56710.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN56710.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56710.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:KQN56710.1}.
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DR EMBL; LMLK01000021; KQN56710.1; -; Genomic_DNA.
DR RefSeq; WP_056236677.1; NZ_LMLK01000021.1.
DR AlphaFoldDB; A0A0Q4MW90; -.
DR STRING; 1736225.ASF13_06205; -.
DR Proteomes; UP000050856; 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 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:UP000050856};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 287..486
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 306
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 533 AA; 55814 MW; E518506230498D62 CRC64;
MTDEIASLFP SGEFTAFDFT RPEYAEPPLA GSPLIGLHSL CGKVTLSNAL CCDVQLLESD
GAVALAGKSA GGQGLTGSAP LVSQPDSLLS FSYRYLDPAT MQRVIWQQAT GAVARLQIVQ
NGAFNGVALA HLPTLLGVFI AGASGGKGAG GMPQPVAVSP GVWHRVQLVL SAQPDASRLI
VDGREIDTFT LSAIPATPFT LFGTVGRQVP SSPLLLGRIV ATSPLPAEPV IAKIQAWLAA
GYKPGGASSP AGRPEKYNPR ALHPVSQVSV TTSQARVAAI INHDGSINPE KVLIADGENA
IHPLASLTKI MTAIVLLDGQ PEYSEKLTRL SCDPATGSGA NLAEGDTLCL RDAVYNLMLP
SSNVTANMVA RIYGGKLLTA EGQSGYSVPQ AVSRWVAQMN SRAQALGMHS ARFTTPSGLG
RNSASALDVL KMVAAATQYP LIMQSWRTQT HAIKVSGNAP RLEYIINTND LLFSDPTVIG
GKTGTLTPLF NLFCLAQMPD HQRLVVIALA ASAKQDRATD CAAMLAAIKA QYD
//
