ID A0A0B4Y1K2_9PROT Unreviewed; 399 AA.
AC A0A0B4Y1K2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AJD52528.1};
GN ORFNames=TH3_12060 {ECO:0000313|EMBL:AJD52528.1};
OS Thalassospira xiamenensis M-5 = DSM 17429.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1123366 {ECO:0000313|EMBL:AJD52528.1, ECO:0000313|Proteomes:UP000007127};
RN [1] {ECO:0000313|EMBL:AJD52528.1, ECO:0000313|Proteomes:UP000007127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M-5 {ECO:0000313|EMBL:AJD52528.1,
RC ECO:0000313|Proteomes:UP000007127};
RX PubMed=23209216; DOI=10.1128/JB.01904-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of Thalassospira xiamenensis type strain M-5.";
RL J. Bacteriol. 194:6957-6957(2012).
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; CP004388; AJD52528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4Y1K2; -.
DR STRING; 1123366.TH3_12060; -.
DR KEGG; txi:TH3_12060; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_1_1_5; -.
DR Proteomes; UP000007127; Chromosome.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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 Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
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 Pfam; PF05036; SPOR; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF110997; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AJD52528.1};
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:AJD52528.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002112289"
FT DOMAIN 311..399
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT ACT_SITE 46
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 399 AA; 43383 MW; A58D98494FF861FA CRC64;
MLLIIAAVVF TTPAAMARTY TAMVIDAETG DVLHEYRADH KVYPASLTKI MTLYMLFDAL
DSGKVSLSTR MEVSKRAWGQ APSKLGLQPG EKISVEDAIL ALVTKSANDI AVVVAEHLGG
TEVKFAQMMT AKARQIGMKN TTFRNASGLP NRGQLTTARD MIRLAVSLRK DYGNYYHYFS
TQKFSYGKRT YGNHNNLLAS YYGTDGIKTG YINASGFNLV ASVNRNGRRL IGVVFGGRTA
RSRDDQMKKL LDQAYLELKK DGEIIAPRPR ISPDGKILPA DTQLLMAKQN NANEVEQPGR
IDTETVVARL SPETGGWGIQ VGAFSDQRRA QEAVLAAART APEVLRLTRA AVEQQSNGSG
VVYRARLLGF GGEQEARSAC AALRKEKVAC IPVNAGDAG
//
