ID A0A0C1JAZ9_9RHOB Unreviewed; 468 AA.
AC A0A0C1JAZ9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KIC45362.1};
GN ORFNames=RA28_13005 {ECO:0000313|EMBL:KIC45362.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC45362.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC45362.1}.
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DR EMBL; JWLK01000004; KIC45362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1JAZ9; -.
DR STRING; 1577904.RA28_13005; -.
DR Proteomes; UP000031326; 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:KIC45362.1};
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:KIC45362.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031326};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 31..253
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 60
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 468 AA; 50258 MW; 87ECB7B0980BE1E9 CRC64;
MQVRRTVPAR MGFLLIVLMW VLSFAPMQVT AAPYAAMVID ARTGEVLHSR NADTRLHPAS
LTKMMTLYIA FEAVRNGEIT LDTPVRITKK AASEPPSKLG LRSGQTIAFR YLIRAAAVKS
ANDAATAIGI ALSGSEAAFA RRMTRTAKAM GMSRTTFKNA HGLTESGHMS TARDMTTLGR
HLLYDYPQYY NLFSRKSTDA GIKTVPNTNR RLLAAYKGAD GIKTGYTRAA GFNLVASAKR
KDERIIATVF GGKSGASRNA RVAELLDMGF RRAPSRAPIR KPSRPAYAGN AGLEGAVKVA
RLTAAPKSSL RPVLRPGPGT AIQVAGTVAE TAAKNGSRIQ NGIAAAIAAA DIKPSDATGQ
AEETQVVASV EPVKQPEPEP EVVTRLSTSG GHLWGVNVGR YTTRYEAEKV LLKTALSEMT
TLEGTLRKVN KSTRGFDATF QGMTREQADL ACRRLQARNV TCFMIGPS
//
