ID A0A0G1GWJ1_9BACT Unreviewed; 338 AA.
AC A0A0G1GWJ1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Penicillin-binding protein dacF {ECO:0000313|EMBL:KKT38583.1};
GN ORFNames=UW27_C0001G0079 {ECO:0000313|EMBL:KKT38583.1};
OS Parcubacteria group bacterium GW2011_GWA1_44_13.
OC Bacteria.
OX NCBI_TaxID=1618788 {ECO:0000313|EMBL:KKT38583.1, ECO:0000313|Proteomes:UP000034180};
RN [1] {ECO:0000313|EMBL:KKT38583.1, ECO:0000313|Proteomes:UP000034180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 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:KKT38583.1}.
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DR EMBL; LCHR01000001; KKT38583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1GWJ1; -.
DR Proteomes; UP000034180; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; 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 GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..320
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 101
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 338 AA; 36179 MW; 6113DD24B4541A7A CRC64;
MNTKKDREKI ITRRAHSLLV VLGGGAGLAI AMQGLLSFAL PAQTETSVNN AGDAREEIRT
AKIANPFDGI SLEARAGYVL ELKTGVVLFA KNENEKLPLA SVTKLMTAFV AREHLSESAV
LTLTKDDLSA EGDSGLRPGE RWRLGDILNA MLLVSSNDAA HAVALFVGSN GVSDRNASTD
IARANFVQMM NEKAVLLGLE QMQFFNESGL DVSAPQSGQL AQVSILPQGG GYGSARNVAL
LFAELWKKYP ETIEITAHKD ARIYSQDEIA HILPNTNEIV GQIPGLVASK TGYTNISGGN
LAVIFDRGIG DPIVAVVLGS SYKGRFDDMQ KLVEATRK
//
