ID R9KQ34_9FIRM Unreviewed; 481 AA.
AC R9KQ34;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=C809_02117 {ECO:0000313|EMBL:EOS48438.1};
OS Lachnospiraceae bacterium MD335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS48438.1, ECO:0000313|Proteomes:UP000014081};
RN [1] {ECO:0000313|EMBL:EOS48438.1, ECO:0000313|Proteomes:UP000014081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COE1 {ECO:0000313|EMBL:EOS48438.1,
RC ECO:0000313|Proteomes:UP000014081};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL Submitted (APR-2013) 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:EOS48438.1}.
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DR EMBL; ASSW01000039; EOS48438.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KQ34; -.
DR STRING; 1235793.C809_02117; -.
DR PATRIC; fig|1235793.3.peg.2183; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_567159_0_0_9; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000014081; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; 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 GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 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:UP000014081};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 191..425
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 216
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 481 AA; 52751 MW; C1A834AFD21306D8 CRC64;
MKKTIRKINS VILSVILVCL IFPVRASASY EIPKTCQVQT DTGAAYTVKT LDYSYDCNTY
FSMRDIAVAL NGTDKSFSLE ITKNAVSLTP GSAYTPVGVE NIPWEDVENP DISLRRNEMK
VNGQEVRYYT LIMALPSGHY DCFMMAADLA MILDMNITVS EAGVLQLQTQ APFRIDPAAL
EQAGYFYGVN SVLVGDAATG EYYYQYQSDI SYPIASTSKL MTCLLAMEAI SEGRLSLEEP
VIISEAVQAL SASDDGVIPL ETGEQITVQE LLLGALLPSS NECALCLAEA IAGSEEAFVE
KMNQKALDLG LSQAIFFNCN GLPSYTQEPI PAKRQNRMSA EDMFRLVSYL LRVYPQVTDM
TSLQSATLQS LDLEVRNTNP LLHNLPEVTG LKTGTTNKSG ACLVTSLTVD DGNMKHDLIV
IVLGTEDSIE RGRVSELLAK YALQVFDTGM EETKNEALPQ NLPTHARAAV DWILRTARTK
Q
//
