ID A0A136JSD2_9BACT Unreviewed; 340 AA.
AC A0A136JSD2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacF {ECO:0000313|EMBL:KXK00072.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KXK00072.1};
GN Name=dacF {ECO:0000313|EMBL:KXK00072.1};
GN ORFNames=UZ19_OD1000228 {ECO:0000313|EMBL:KXK00072.1};
OS Parcubacteria bacterium OLB19.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1617425 {ECO:0000313|EMBL:KXK00072.1, ECO:0000313|Proteomes:UP000070365};
RN [1] {ECO:0000313|EMBL:KXK00072.1, ECO:0000313|Proteomes:UP000070365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB19 {ECO:0000313|EMBL:KXK00072.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK00072.1}.
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DR EMBL; JZEL01000012; KXK00072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JSD2; -.
DR STRING; 1617425.UZ19_OD1000228; -.
DR Proteomes; UP000070365; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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 Carboxypeptidase {ECO:0000313|EMBL:KXK00072.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXK00072.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:KXK00072.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..315
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 115
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 340 AA; 36826 MW; 440D4AD80FB3ED14 CRC64;
MNDNEPYIIE TNEVKNEVKT KNNFPVLIQV IVILLLLGGV LSGIAFTNES LSLKDKDKIV
LNANLPVTEI STSTSPVPQK IESVSIIAKS AFVWDVNEQR VLFQKNQDEV LPLASITKLM
TALVAYELLP DDAKVKVTKE AASQQSGGSL REGEVFAVKE LADFALVSSY NSAAFTLADA
VGSELGDRDP VAQFVASMNI RAEELNLNTL KFLNPTGLDI STDEAGAYGS AKDVSFLVEY
ILKNHPAILE PTKSPHTRLY NTDGEFHDAR NTNNILTSIP NLIGSKTGYT DLAGGNLTVT
IDIGFDHPVV ITVLGSTIDG RFADVSKLIE AVQESMINKE
//
