ID A0A1N7BF97_9GAMM Unreviewed; 273 AA.
AC A0A1N7BF97;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Murein-DD-endopeptidase. Serine peptidase. MEROPS family S11 {ECO:0000313|EMBL:SIR50059.1};
GN ORFNames=SAMN05880558_11543 {ECO:0000313|EMBL:SIR50059.1};
OS Aeromonas sp. RU39B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIR50059.1, ECO:0000313|Proteomes:UP000186911};
RN [1] {ECO:0000313|EMBL:SIR50059.1, ECO:0000313|Proteomes:UP000186911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU39B {ECO:0000313|EMBL:SIR50059.1,
RC ECO:0000313|Proteomes:UP000186911};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTMJ01000015; SIR50059.1; -; Genomic_DNA.
DR RefSeq; WP_076577181.1; NZ_FTMJ01000015.1.
DR AlphaFoldDB; A0A1N7BF97; -.
DR STRING; 1907416.SAMN05880558_11543; -.
DR InParanoid; A0A1N7BF97; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000186911; 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..273
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012252850"
FT DOMAIN 27..255
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
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 118
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 273 AA; 30247 MW; A22DF91CC6C3BD1D CRC64;
MGFSLRALGL LGMLAGSLFI APAVAAKPAL QVMSSSALVL DVNSGQTLYQ KNPNQVRPIA
SLTKLMTALV VLDAKQNLND VITVDESDRD LLKGTHSRIR MGTKVTRRDA LHLALMSSEN
RMASALARHY PGGKPAFIRA MNNKARQLGM RSSRFYDSTG LTTRNVSTAR DLSKLVAAAY
RQPLIRQFTQ DTSREMRFNS PAYTLMFNNT NPLVKNSDWD VHLSKTGYTD EAGRCLVMRA
KPDNRELAII LLNAQGKRTP VGDANRIRQW LRS
//
