ID F7SVM3_9BURK Unreviewed; 407 AA.
AC F7SVM3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EGP47804.1};
GN ORFNames=AXXA_03589 {ECO:0000313|EMBL:EGP47804.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP47804.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP47804.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP47804.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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:EGP47804.1}.
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DR EMBL; AFRQ01000028; EGP47804.1; -; Genomic_DNA.
DR AlphaFoldDB; F7SVM3; -.
DR MEROPS; S11.002; -.
DR PATRIC; fig|1003200.3.peg.687; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_0_0_4; -.
DR Proteomes; UP000004853; 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 Carboxypeptidase {ECO:0000313|EMBL:EGP47804.1};
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 Protease {ECO:0000313|EMBL:EGP47804.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 151..378
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 14..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 407 AA; 42119 MW; 995A1DB187A5AD13 CRC64;
MCALLPSAAL AAKNTDPCKT NAKSAACKAQ QAKKAPAPAK AGTGKVAAPK QAAGKAAPKA
AAGKQAAPKS AAAKAPPKGA AGKQAAAKGA PKQAAGKKAP PKGGKQAVAQ QSSSKKGAAG
KNGKPNKPSR AQRTAAAAAA AAMPPPAVSV RAEAAALRSS TAYVQDLATS TVIFAKNENV
VRPIASISKL MTAVVVVDAN QPMDEMLEIT DEDIDGLKHT TSRLRVGTKL SRGDMLHLAL
MSSENRAANA LGRHYPGGLP AFVAAMNAKA QSLGMTSTHF IEPTGLSSNN VSSPHDLARL
LRAASQRPLI HRYSTDTEYD VEINNRTQTF RNTNLLVRKP DWDIKVSKTG YINEAGECLV
MLARINGRDL AIVLLDSQGK LSRIGDAVRI RRIVQSEVAM ASAQPGG
//
