ID A0A1F6PDV9_9BACT Unreviewed; 346 AA.
AC A0A1F6PDV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A2538_00845 {ECO:0000313|EMBL:OGH94339.1};
OS Candidatus Magasanikbacteria bacterium RIFOXYD2_FULL_41_14.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798709 {ECO:0000313|EMBL:OGH94339.1, ECO:0000313|Proteomes:UP000178254};
RN [1] {ECO:0000313|EMBL:OGH94339.1, ECO:0000313|Proteomes:UP000178254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH94339.1}.
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DR EMBL; MFRE01000009; OGH94339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6PDV9; -.
DR STRING; 1798709.A2538_00845; -.
DR Proteomes; UP000178254; 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; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..312
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 117
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 120
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 346 AA; 38378 MW; BDD633EFF9C9467D CRC64;
MTEEKQKSIK DFFLSFSIML CGVGLLFIGS VSFVPTSTIT SNTVATFPQS APRQNLLVGG
DVTPTVLPVS HPLVPLAKLD KKEFEQPLTA AAALVVDNHT DTELFSQNAD VARPLASITK
LMSMLVILER RLDWNAKTTI TADEIEGSHI VEADEVYTAE ELWNLALVGS ANGAVNALVR
LSSYTRSEFV ARMNTKAKIW RLDSMNFVEP TGLDSGNVGN TRDVARLLKF ALREDKIYRT
LQIPEYYARP EGAAKARRVW STDWLLTGWV QNKFDTEQMA GKTGYITDSN YNFTVKLGDA
EGRAVRVVIL GATNHEARFT EARDLAVWAF ANFLWPEDSG YGELVE
//