ID A0A258C765_9GAMM Unreviewed; 233 AA.
AC A0A258C765;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:OYW91429.1};
DE Flags: Fragment;
GN ORFNames=B7Z23_08170 {ECO:0000313|EMBL:OYW91429.1};
OS Pseudomonadales bacterium 32-61-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX NCBI_TaxID=1970544 {ECO:0000313|EMBL:OYW91429.1, ECO:0000313|Proteomes:UP000215582};
RN [1] {ECO:0000313|EMBL:OYW91429.1, ECO:0000313|Proteomes:UP000215582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-61-5 {ECO:0000313|EMBL:OYW91429.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYW91429.1}.
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DR EMBL; NCDF01000520; OYW91429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258C765; -.
DR Proteomes; UP000215582; 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 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 2..179
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYW91429.1"
SQ SEQUENCE 233 AA; 25811 MW; 1694DA430FE58DD6 CRC64;
PLDEYLTITI RDAVEMKGVF SRVRIGSEIS RREMLQLTLM SSENRAAASL AHHYPGGYAA
FIQAMNLKAS ELGMSSTRYV EPTGLSERNV SSANDLVKLL RASQAYPLIE QLSTRSEKTV
AFRKPNYTLG FRNTNALVRK PNWDIQLSKT GFTNAAGHCL VMRTVMDQRD VAFVVLDAFG
KYTHMADANR LKKWLETGKA TPVAPAALAY KAQKQVERRL AGQPGNAAMA EAR
//
