ID A0A0L1JRT5_9RHOB Unreviewed; 467 AA.
AC A0A0L1JRT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=ATO11_07695 {ECO:0000313|EMBL:KNG94436.1};
OS Pseudaestuariivita atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudaestuariivita.
OX NCBI_TaxID=1317121 {ECO:0000313|EMBL:KNG94436.1, ECO:0000313|Proteomes:UP000036938};
RN [1] {ECO:0000313|EMBL:KNG94436.1, ECO:0000313|Proteomes:UP000036938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z3 {ECO:0000313|EMBL:KNG94436.1,
RC ECO:0000313|Proteomes:UP000036938};
RA Li G., Lai Q., Du Y., Liu X., Sun F., Shao Z.;
RT "Aestuariivita atlantica sp. nov., isolated from deep sea sediment of the
RT Atlantic Ocean.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(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:KNG94436.1}.
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DR EMBL; AQQZ01000003; KNG94436.1; -; Genomic_DNA.
DR RefSeq; WP_050530594.1; NZ_AQQZ01000003.1.
DR AlphaFoldDB; A0A0L1JRT5; -.
DR STRING; 1317121.ATO11_07695; -.
DR PATRIC; fig|1317121.7.peg.2146; -.
DR Proteomes; UP000036938; 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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000036938};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 6..224
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 31
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 467 AA; 49962 MW; 977855CA8C996303 CRC64;
MAAPYAAMVM DARTGEVLHS RNADSRLHPA SLTKMMTLYV VFQAVENGEV SMDTLIRVSK
KAASEPPSKL GLRAGQKIKL RYLVRAAAVK SANDASTAIA EGLAGSEAAF ARRMNRTARA
LGMTKTTFKN AHGLTEAGHL STARDMTILG RHVIYDYPQY YNLFSRKTAD AGVRTVSHTN
HRLLSSYKGA DGIKTGYTRA AGFNLVASAE RGRERVIATV FGGRSTTTRN ARIAELLDMG
FKRAPTRVAF RAPRKPTYHA APAPKVVAGR KTGPGTAGKT IRVSGLVTKS LRPKRRPIPE
TAPVVVAAQD DLKDALAEAQ TLPSPDTVAA AAEQAIKAAE EAPAKSIKPV MRPKELVLAS
AKPAPRAPSV SADTSEAVQE VVTRLSASGG RHWGVNVGRY GSRFQAEKVL LKTALAEMTV
LDGSLRKVVK RKGGFDANFM GLTRESADLA CRRLQGRGVT CFMIGPS
//