ID A0A3S0L1E5_9PROT Unreviewed; 446 AA.
AC A0A3S0L1E5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:RTR24319.1};
GN ORFNames=EJ903_00605 {ECO:0000313|EMBL:RTR24319.1};
OS Azospirillum griseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2496639 {ECO:0000313|EMBL:RTR24319.1, ECO:0000313|Proteomes:UP000277007};
RN [1] {ECO:0000313|EMBL:RTR24319.1, ECO:0000313|Proteomes:UP000277007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-25-5w-1 {ECO:0000313|EMBL:RTR24319.1,
RC ECO:0000313|Proteomes:UP000277007};
RA Yang Y.;
RL Submitted (DEC-2018) 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:RTR24319.1}.
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DR EMBL; RXMA01000001; RTR24319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0L1E5; -.
DR OrthoDB; 9795979at2; -.
DR Proteomes; UP000277007; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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 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:RTR24319.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:RTR24319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277007};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..279
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 362..440
FT /note="SPOR"
FT /evidence="ECO:0000259|Pfam:PF05036"
FT REGION 311..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 147
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 446 AA; 47527 MW; 466F3B10D28F036B CRC64;
MTVTRNTVHN GLFPFAFQAA ETAGERSAWR LTRTLFALGA LVVAGLAGAG LGAAEAEAAK
AASIIMDART GEVLHEQDAD AIAHPASLTK MMTLYLTFDA LEDGRLSLDQ SLPVSSWAES
MSPTKLGLRA GSSLKVENAI LGLVTKSAND AAVVLAEALG GTESRFAEMM TRKARELGMR
HTVYRNASGL PNMEQVTTAR DYAILSRALM SDHAKYYPYF SRRNFVYGGR TLPNHNRLMS
RYEGMDGIKT GYTVASGFNL AASAVRDGRR LVGVVLGGKS PVSRDNRMAA LLDQAFGKPN
RGREDGALVA SAERLSKEEP DAEGDDEDEE DDTAAKVGPK RATVQLASLA TAATAKAAGK
AAEKWGIQVG AFATRAAGQK ALTQANKQAP FLLRGAKTAV LETKNGKDTV YRARMVGMDE
KTARKACSEL NRHGLRCVAV SPGEKL
//
