ID M2TLQ5_9SPHN Unreviewed; 373 AA.
AC M2TLQ5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EMD82666.1};
GN ORFNames=C725_2053 {ECO:0000313|EMBL:EMD82666.1};
OS Pacificimonas flava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Pacificimonas.
OX NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD82666.1, ECO:0000313|Proteomes:UP000011717};
RN [1] {ECO:0000313|EMBL:EMD82666.1, ECO:0000313|Proteomes:UP000011717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2015 {ECO:0000313|EMBL:EMD82666.1,
RC ECO:0000313|Proteomes:UP000011717};
RX PubMed=23661488;
RA Tang K., Liu K., Li S., Jiao N.;
RT "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family
RT Sphingomonadaceae of the Alphaproteobacteria.";
RL Genome Announc. 1:E00226-13(2013).
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:EMD82666.1}.
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DR EMBL; AMRV01000006; EMD82666.1; -; Genomic_DNA.
DR RefSeq; WP_008602542.1; NZ_JACHGC010000008.1.
DR AlphaFoldDB; M2TLQ5; -.
DR PATRIC; fig|1234595.3.peg.2054; -.
DR OrthoDB; 5291989at2; -.
DR Proteomes; UP000011717; 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:EMD82666.1};
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:EMD82666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011717};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 48..269
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 322..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 373 AA; 40106 MW; B116246A8ACA4B68 CRC64;
MTARATTIAG DHADRSLGHR LAASLILLGL LIASAFAQPA DARSLLHLDK YAAIVMDADS
NEVLYARNPD AARPPASITK IMTLMIAFEE IDAGRLNLDD RVYFSATAAS QPPSKLGIGK
GGWITVEQAI RLLTTKSAND VAVALAERIE GTEVAFAQRM TEKARSLGMN ATSFYNASGL
PHAGHITTAR DLATLSSALI HQFPHYYAYF SAQSYTMDGQ TFPNHNRLLG ELVGLDGIKT
GFTNAAGFTL AASAQRDGKR LIAIVLGAPS SAARNENITE LINSGFEVLK QRRYGRNTTV
ASFMKEPEPS VVDLWSQPAT AQGSALDEDA EPTFKPTASL KSGGVSQPQE LSRAYAFTPF
STSLMFQSYA WLR
//
