ID B7J6B7_ACIF2 Unreviewed; 323 AA.
AC B7J6B7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase, putative {ECO:0000313|EMBL:ACK78815.1};
GN OrderedLocusNames=AFE_2350 {ECO:0000313|EMBL:ACK78815.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK78815.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK78815.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP001219; ACK78815.1; -; Genomic_DNA.
DR AlphaFoldDB; B7J6B7; -.
DR STRING; 243159.AFE_2350; -.
DR PaxDb; 243159-AFE_2350; -.
DR KEGG; afr:AFE_2350; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_1_2_6; -.
DR Proteomes; UP000001362; 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; 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:ACK78815.1};
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:ACK78815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001362};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 57..281
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 89
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 323 AA; 35422 MW; 33F6D6AFC9E091C7 CRC64;
MRRGVPMLAS IPVPDTDFGP STVKYFPSTG WWLFSWLSLV AIFLFCIPRA EAETSGLPPI
DARAYILMNA DTGAIIATKN AYRPYAIASI TKLMTLYLLF KDIDSGHLQL NQHFVPCRAA
LQTGGSSMFM HPGMPFTIAQ LILGMTVPSG NDAAVETAHL VAGSVPAFVA EMNRTARKIG
MLSTTFYDPD GLPHPNNMAS PYDVAVLTRT LMTQFPQFMP FFRHENFTYA GITSPNPNLL
VGRVPFITGM KSGYTDAAGH CLVATGTQNG ISLIAVILGV PSFRDEGRGF WRASWQSLKL
LDWGFARTLW LPSVPHLERT SAR
//
