ID A0A0U5MCD3_9PROT Unreviewed; 429 AA.
AC A0A0U5MCD3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase(Beta-lactamase/transpeptidase-like, 14-271) {ECO:0000313|EMBL:CUW38420.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:CUW38420.1};
GN ORFNames=XM1_1351 {ECO:0000313|EMBL:CUW38420.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW38420.1, 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; CUW38420.1; -; Genomic_DNA.
DR RefSeq; WP_068431418.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5MCD3; -.
DR STRING; 1663591.XM1_1351; -.
DR KEGG; magx:XM1_1351; -.
DR PATRIC; fig|1663591.3.peg.1352; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000063191; Chromosome I.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
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 Pfam; PF05036; SPOR; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CUW38420.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUW38420.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:CUW38420.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006861794"
FT DOMAIN 36..253
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 347..422
FT /note="SPOR"
FT /evidence="ECO:0000259|Pfam:PF05036"
FT REGION 323..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 429 AA; 45307 MW; D1BECD7C96C5AF2A CRC64;
MHLSRIGFLN RVRLFAVALA AILTLSAQPA LAGRYASIVI DAESGSVLHA ASPDAKSYPA
SLTKVMTLFL LFDELDSGRI RLDTKFTTSA HAAAQSPSKL GLEPGEKISV ESLILALVTK
SANDAAVVAA EGVGGTEANF AQMMTRKAHA LGMRSTTYRN ASGLPDLGQV STVRDQATLA
RALIRSHPGY YKYFSTRQFV YDGQPINTHN RLMLRYQGAD GIKTGYIHAS GFNLISSAKR
GDRRIIGVVF GGNTAASRDK HMGQLLDKGF AKLRKGESVE MAEAEADDLP DLDELVAAAQ
AAKAPAKAKA KVAAKPVPAK KVAMRAPARA AANDDDDDDD AVGDADPASW AIQVGAFNEY
RPAHKAASDA AKKLGGLVSK ASIDIDKAGK GAKTVYRARI SGFTEDQARA ACKRLGKAGK
ACKPVNPNT
//
