ID C9MZD2_9FUSO Unreviewed; 423 AA.
AC C9MZD2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:EEX74120.1};
GN ORFNames=GCWU000323_01929 {ECO:0000313|EMBL:EEX74120.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX74120.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX74120.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX74120.1,
RC ECO:0000313|Proteomes:UP000006233};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX74120.1}.
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DR EMBL; ACVB02000018; EEX74120.1; -; Genomic_DNA.
DR AlphaFoldDB; C9MZD2; -.
DR STRING; 634994.GCWU000323_01929; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_1_2_0; -.
DR Proteomes; UP000006233; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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 Carboxypeptidase {ECO:0000313|EMBL:EEX74120.1};
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 Protease {ECO:0000313|EMBL:EEX74120.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006233};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 51..271
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 423 AA; 46255 MW; 40BA2D6CE1975989 CRC64;
MDNEKRLKGI KMKKKLNIGR RSKKIIMSMA FLTVSALSFA SGEDYYDYKS LLIGDINGNI
IKEDNSSAVR PLASVTKIMT SILTLDKIKN GQISYEDKVT VSAKAASVPY GIKLTAGKQY
TVRDLLKATI IKSSNNAAYA LAEYVGGDVS NFVHSMNEKA RSYGLNSLRY CSPHGLPPSY
TGSCMDQGNA KDLYKLAQIT LKDYSEYLNF SKNKTDYVDN GNTKVTSTNA LLGNVLGVDG
IKTGYHDAAG SNIVLTANRG NDRMIAIILG SNRAKDRNAI GAKEINDYYA NGYARKASVK
NNSLRPIEST YNTDNTETSK NSKGNSKVDQ FFNMIFGKNH NNSAGKKMKI INKNDVVATA
TIGDVKYNLY PTKDVEITAT ERPNLTYSVN LNSGVTKESR GKIVGTYVAT DGTLTYSGEL
IMK
//
