ID A0A1I6J617_9BURK Unreviewed; 343 AA.
AC A0A1I6J617;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Murein-DD-endopeptidase. Serine peptidase. MEROPS family S11 {ECO:0000313|EMBL:SFR74439.1};
GN ORFNames=SAMN05428960_0928 {ECO:0000313|EMBL:SFR74439.1};
OS Mitsuaria sp. PDC51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR74439.1, ECO:0000313|Proteomes:UP000199246};
RN [1] {ECO:0000313|EMBL:SFR74439.1, ECO:0000313|Proteomes:UP000199246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC51 {ECO:0000313|EMBL:SFR74439.1,
RC ECO:0000313|Proteomes:UP000199246};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOZE01000001; SFR74439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6J617; -.
DR STRING; 1881035.SAMN05428960_0928; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000199246; 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 Reference proteome {ECO:0000313|Proteomes:UP000199246};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..343
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011584543"
FT DOMAIN 72..297
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 343 AA; 36282 MW; 53C33DC59595918E CRC64;
MLLTGLTASL LPVQPAQAAT ASSSKAKVKS VRKAKPAPRS PRKVAARAAA PAREVALSKP
SFGTMYGLHD TEDPLDLKSS VAYVVDQDTN EVLFSKNPSA VLPIASITKL MTALLVVEAN
QSLDEKLEIT DEDKDTEKFT GSRLAIGTEL TRGELLHLAL MSSENRAAHA LGRNYPGGLE
AFVAAMNAKA RALGMMDTHY VEPTGLSSRN QSSAADLAKL VKVAHAFPLI RELSTSSEYT
VALGRRQVRF GTTNGLVRKG DWDIGLQKTG FINEAGQCLV MQAQLAGRKL IMVFLDSAGK
YSRIGDAERV RKWLTGAASP LAGVATAPAA ATTAAVIPAV SAK
//
