ID F6ADI4_PSEF1 Unreviewed; 302 AA.
AC F6ADI4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:AEF20125.1};
GN OrderedLocusNames=Psefu_0139 {ECO:0000313|EMBL:AEF20125.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF20125.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF20125.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP002727; AEF20125.1; -; Genomic_DNA.
DR RefSeq; WP_013789268.1; NC_015556.1.
DR AlphaFoldDB; F6ADI4; -.
DR STRING; 743720.Psefu_0139; -.
DR MEROPS; S11.002; -.
DR KEGG; pfv:Psefu_0139; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_0_3_6; -.
DR OrthoDB; 5688590at2; -.
DR Proteomes; UP000000686; 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: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 Carboxypeptidase {ECO:0000313|EMBL:AEF20125.1};
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:AEF20125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..302
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003330976"
FT DOMAIN 27..257
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 63
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 302 AA; 32853 MW; C1660A4B5E3B79B9 CRC64;
MNIRRPFASL ALACLFIVSP LVATAATAPA KQELASGSAL LVDLNTNKVL YSSNPDMMVP
IASVTKLMTA MVTLDAKLPL NEELPVIIRD VHEMRGVYSR VRIGSEISRR EMLLLTLMSS
ENRAASSLAH HYPGGVTAFV AAMNAKARAL GMTHTRYVEP TGLSEHNVST ANDLVKLLKA
TRSYPLIGEL SSTPEKTVAF HKPNYTLGFR NTNGLTRKQG WDVQLTKTGF TNSAGHCLVM
RTTMAGKPVA FVVLDAFGKY THMADASRLR KWVETGKVTP VAPAALAYKQ QRAAQRQLQA
SQ
//
