ID C7N631_SLAHD Unreviewed; 464 AA.
AC C7N631;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ACV22366.1};
GN OrderedLocusNames=Shel_13430 {ECO:0000313|EMBL:ACV22366.1};
OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS RHS 1) (Peptococcus heliotrinreducens).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22366.1, ECO:0000313|Proteomes:UP000002026};
RN [1] {ECO:0000313|EMBL:ACV22366.1, ECO:0000313|Proteomes:UP000002026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC {ECO:0000313|Proteomes:UP000002026};
RX PubMed=21304663; DOI=10.4056/sigs.37633;
RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT 1).";
RL Stand. Genomic Sci. 1:234-241(2009).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP001684; ACV22366.1; -; Genomic_DNA.
DR RefSeq; WP_012798468.1; NC_013165.1.
DR AlphaFoldDB; C7N631; -.
DR STRING; 471855.Shel_13430; -.
DR KEGG; shi:Shel_13430; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_7_3_11; -.
DR Proteomes; UP000002026; Chromosome.
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; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
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; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 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:ACV22366.1};
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:ACV22366.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..49
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 50..464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002978911"
FT DOMAIN 72..310
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 103
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 464 AA; 50029 MW; 0DEA3E7E861617F1 CRC64;
MTDRTNATYS NSESFALLAP SVRAAVVLAA ACAAAIFACL FASSSPAYAS VEDDDIIMGQ
TVEARGVSAK YCPDISSECA IVVGDDGTVY YERNADQQHQ IASITKIMTA IVALENADLN
TEVTVSKASA TVGESSANLK EGDTMDLRTA LMCLLIPSGN DAGIAIAETV GTIMDPSASD
PQAVFVSAMN AKAEELGCTN THFTNPHGLD ADKWGSDMHS SARDVVTMAR YAMSYDTFAE
IVQMGDTTVT VTGKDNKARD NWLDATDDLL EEYEGMRGVK TGSSVLADFC FSGCVTRGDE
TFYTVVLGNA TSDERFGDTI TLMDWAFGST VHTDFINSDF VISEEDPRPY VADVTLLDWP
NRTVKATVDD EGEVFDLFLP EGDIEQVVSY VRIMGDVEKG DIVGRLEFHR NGQTLKVVQL
IAAEDVAAPT FTESQYNNFD RFRRMMEGAE TPAPSACYNK AIPA
//
