ID A0A1Q7UR02_9CHLR Unreviewed; 317 AA.
AC A0A1Q7UR02;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=AUG82_05050 {ECO:0000313|EMBL:OLE05214.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE05214.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE05214.1, ECO:0000313|Proteomes:UP000186213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLE05214.1}.
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DR EMBL; MNIY01000098; OLE05214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7UR02; -.
DR STRING; 1805225.AUG82_05050; -.
DR Proteomes; UP000186213; 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:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..317
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_5012186571"
FT DOMAIN 54..285
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 87
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 317 AA; 34037 MW; 23FDAD07A53F7ADA CRC64;
MKRRILASIL FFLAIELALA APVLAFTPFG TRLLQEIVPP PTPSPTPILT VRGTPPSTSA
QAAYLLDTDT GHVLVDVRGE QRLPMASTTK IMTALIAIQT ADLSQLVTIR QDAIKEVQAH
NGSTANLVVG DQISLKDLLY GLMLPSGDDA AVAIADAVGG TTSKFVQTMN LFARRLHLTQ
THYINPDGLT YLTPQGRPDP NQYMSAADLV HLARSAMANP FFAQIVELQH FVLPASTVHH
AYAWDSINTL LSTYPGATGI KTGYTVEAGY CLVFAATNGG HHLLGALLHE PDANQRFVDA
RALLDWGFAL PLIPPAS
//
