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Database: UniProt
Entry: I2BBA0_SHIBC
LinkDB: I2BBA0_SHIBC
Original site: I2BBA0_SHIBC 
ID   I2BBA0_SHIBC            Unreviewed;       403 AA.
AC   I2BBA0; K6VWC1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   Name=dacA {ECO:0000313|EMBL:AFJ47804.1};
GN   OrderedLocusNames=EBL_c27330 {ECO:0000313|EMBL:AFJ47804.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ47804.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ47804.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP001560; AFJ47804.1; -; Genomic_DNA.
DR   RefSeq; WP_002439196.1; NZ_BAHA01000001.1.
DR   AlphaFoldDB; I2BBA0; -.
DR   STRING; 630626.EBL_c27330; -.
DR   MEROPS; S11.008; -.
DR   KEGG; ebt:EBL_c27330; -.
DR   PATRIC; fig|630626.3.peg.2648; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_8_1_6; -.
DR   OMA; MYPASIT; -.
DR   OrthoDB; 9795979at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001955; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
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:SF27; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 1.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:AFJ47804.1}; 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:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..403
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003655203"
FT   DOMAIN          292..383
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   ACT_SITE        73
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   403 AA;  44126 MW;  2DD575641DEC95BF CRC64;
     MKNVLPVRIA KGVTLSLTIG LMAMSAARAD DLNIKTMIPG VPQIDAEAYI LIDYNSGKIL
     AEQNADARRD PASLTKMMTS YVIGQAMKAG KFKESDVVTI GPDAWATGNP VFKGSSLMFL
     KPGMEVPVSQ LIRGINLQSG NDACVAMADY VAGSQDAFVG LMNSYVNALG LKNTHFQTVH
     GLDAQGQYSS ARDMALIGQA LIRDVPNEYA IYKEKEFTFN GIRQPNRNGL LWDNSLKVDG
     IKTGHTSSAG FNLVASATEG QMRLISAVMG GHTSKGREAE SKKLLTWGFR FFESVNPLKA
     GKEFASEPAW FGDSDRASLG VDKDAWLTIP RGRMKDLKAS YVLNNTELHA PLQKNQVVGT
     INFQLDGKII DQRPLVVLQP IEEGNFFGRI IDYIKLMFHH WFG
//
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