ID D9SWS4_CLOC7 Unreviewed; 454 AA.
AC D9SWS4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:ADL51285.1};
GN OrderedLocusNames=Clocel_1537 {ECO:0000313|EMBL:ADL51285.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51285.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL51285.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002160; ADL51285.1; -; Genomic_DNA.
DR RefSeq; WP_010077508.1; NC_014393.1.
DR AlphaFoldDB; D9SWS4; -.
DR STRING; 573061.Clocel_1537; -.
DR KEGG; ccb:Clocel_1537; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_7_3_9; -.
DR OrthoDB; 1701915at2; -.
DR Proteomes; UP000002730; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:ADL51285.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:ADL51285.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..454
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003128501"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..269
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 121
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 454 AA; 50276 MW; A15ED3F433DE73FE CRC64;
MKKQLLSLLM ASTMLLSFSK TTFAEPIPEP QIVGKYAITV DASTGEVIYA KDPDARVYPA
SVTKVMTAIL VEKLFKIDDM VTYTQTAKIQ DPSSINMDIV DIPIGQQIPV SAALKAMMLY
SANDMTELVA TNYPTKGSDS NKEFVALMNS EAKVLGMNST NFVTTNGLDD NTNEHLTTAY
DLSIMAREAA KYPNIRAVWQ LPNPTNIDFP GLTSVQVGNP NKFLQQGTDF YDPSCVGVKS
GFTDKAGRCL LSVFERNGRQ IVGIVLNCET SYLNQTIYTD MKNIINYSYQ AQRSLLTTTE
PATGKVTSYS KDSLLTTIPV EYKEYITWGK TKTIDVPVYL AEDASIYSNA FNLSSLNVKY
NYDIDLFKDD EKNIIGTVTI QERERTTNIP IYTNINSSVM KTLTKTVLPS LSKSTSNSIY
IYTAVASLSV AVITLGVIVH RNRKVKRNTK NKSL
//
