ID A0A1F6NC36_9BACT Unreviewed; 736 AA.
AC A0A1F6NC36;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A3I29_02525 {ECO:0000313|EMBL:OGH81253.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPLOWO2_02_FULL_44_11.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798689 {ECO:0000313|EMBL:OGH81253.1, ECO:0000313|Proteomes:UP000178726};
RN [1] {ECO:0000313|EMBL:OGH81253.1, ECO:0000313|Proteomes:UP000178726}
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:OGH81253.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFQK01000007; OGH81253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6NC36; -.
DR STRING; 1798689.A3I29_02525; -.
DR Proteomes; UP000178726; Unassembled WGS sequence.
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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..736
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009525744"
FT DOMAIN 481..709
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 507
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 510
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 563
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 678
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 736 AA; 83479 MW; 4B7C1E3C518B87A4 CRC64;
MHRKIISYFI VVVSILSPFH VLAQTDFNPH FIISDPELED YQSWTRHDIQ QFLISRGSYL
KNYAAENVSG TIKMASDIIY DAAQRYKINP KFLLVTLQKE QSLITDDTPA EKQLNWATGY
AVCDSCNLED PKILKFKGFG KQVDNAAGIM RWYYDNRDKD FIKKKDLATT IDNQLISPQS
WATAFLYTYT PHIHGNQNFW RIWNTWFEQV YPNGTLIVSA SSTEYWLIDN GQRRKFKNKT
TLITRTDPKT AVTMSEVDLS NYKIGAEISF PNYSLLHTTD KTFLLDHDTL RPFASEAIVG
KLGFNPQELI DVDEFELAGL TIGSTITATS TAPQGVVYYI PEIKSYYFLK DNILYPIVDK
AILTSAYKNV PIENHKLKDL AKFETAERLA MFNDGTLLKD KENQTIYVMD QGKKRPIADD
DTFIALGYKS SNITTAAHLT LANIPTGETI FLNASLLSSR NKYLGDSRAE IPDIYTKNNL
SAYLVAEYPS SRIISGKNID SRQPIASLTK ILTVNEVLNN NVSLDQTTIY NPKLHATYSN
PLRFQTGDKL KNKDLLNAMM VVSNNTASRM LALATKMDET TFVEKINKRL EEWGADNTTI
ADVTGLDENN KSTARDLLKI FTKVLNNDTI RVALGQATYP FSKTSAKNKT EKWTLHNTNQ
IIFKIPFAKR HYKVVATKTG YTDEAKATLL MLIEDKVTKK QYIVVTLGNP DYAKRFQEPH
KIAEWITTSK VSVAGN
//
