ID A0A0U5FV48_9PROT Unreviewed; 417 AA.
AC A0A0U5FV48;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CUW40114.1};
GN ORFNames=XM1_3053 {ECO:0000313|EMBL:CUW40114.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW40114.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-2015) 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; LN997848; CUW40114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5FV48; -.
DR STRING; 1663591.XM1_3053; -.
DR KEGG; magx:XM1_3053; -.
DR PATRIC; fig|1663591.3.peg.3013; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000063191; Chromosome I.
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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:CUW40114.1};
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:CUW40114.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 31..248
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 277..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 417 AA; 43315 MW; A98EA0197C931F43 CRC64;
MAKGQGRYVR YLAGAILGLV LPTAAAWAEP SAFLAVDLGS GAVIAESRGG AAHHPASLTK
MMTAYVAFAA IKAGKVSVDD VITVSDRAAS QGGATLDLRK GERITLGAAL KAMIVRSAND
AAVAVAEHVA GSESAFAARM TEEAARLGMT SSSFRNATGM TAAGHLSSPR DMAMLAMAIE
RDFPAFRPLF SSRDTTWKGR VLPTVNGFLG AYAGAEGMKT GFTCSAGYNL VAIAHRGGRR
ALAVVMGAGS SAERLGAIRR LMDQALGAQP AAGRPLSGLA NGGGAPPDRS LESCGIARGG
KSGGPESALG QRRVAPAGWG LEVAFGRDLG KVRRDLDKAH RELRGRLGGG SAMVVIRPRD
GMLRYRGLIV GLAERRAVDT CLAERARVGE ERCLVMTPTM LAGAVEDERR FKMISAH
//
