ID A0A1J4V308_9BACT Unreviewed; 509 AA.
AC A0A1J4V308;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ44_04420 {ECO:0000313|EMBL:OIO31538.1};
OS Candidatus Nomurabacteria bacterium CG1_02_47_685.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1805282 {ECO:0000313|EMBL:OIO31538.1, ECO:0000313|Proteomes:UP000183206};
RN [1] {ECO:0000313|EMBL:OIO31538.1, ECO:0000313|Proteomes:UP000183206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_47_685 {ECO:0000313|EMBL:OIO31538.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:OIO31538.1}.
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DR EMBL; MNVO01000064; OIO31538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4V308; -.
DR STRING; 1805282.AUJ44_04420; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000183206; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR Pfam; PF03734; YkuD; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 134..248
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT DOMAIN 272..438
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 298
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 509 AA; 56279 MW; 1F779627818C78B4 CRC64;
MNRRKLFRYI REAQQSGVGA EEITQLLLDA GWKRSDIEFA FDIISRGRES FLHVHFLHRH
LSPKVSAGAL VAILTLTGLI SGLYARSTLG SNELLVQNGE NGKIIFEYGS WPILENAKFF
EKVKQDFISQ KADFIEADLS SMKLRVYSEG LLATEVPIGS KGREGSWWET PAGLYKIESM
EKSHYSSFGH VYMPWSMQFQ GNFFIHGWPY YADGSPVAQG YSGGCIRLAD KNAESVYRLA
KTGMPVLVFK ESFITNAADT KYAPKSIVPD TVSYLAADLQ NNFVFAEHLS SDQRFIASIT
KLMTALIAVE YINIEREVSI TSPMVATTSI PRLSAGNKTS VLDLLSLLLL ESSNEAALAI
TSPLGQSHFV DLMNRKAATI GMANSRFTDT SGIIATNTST ATDLFMLAKY LYYNRSFVLH
MSMGNENRAA YGPSQYKNLS NLNEISGLEK MIGGKVAESS AAQGGMLAVF KMNVGEEMRP
VAIIVLGSKD SKRDVKTLFD YVQANFDAQ
//
