ID A0A117S789_9SPHN Unreviewed; 474 AA.
AC A0A117S789;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=APF82_04395 {ECO:0000313|EMBL:KUO55413.1};
OS Sphingomonadales bacterium BRH_c42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO55413.1, ECO:0000313|Proteomes:UP000054281};
RN [1] {ECO:0000313|EMBL:KUO55413.1, ECO:0000313|Proteomes:UP000054281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO55413.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:KUO55413.1}.
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DR EMBL; LOEX01000059; KUO55413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117S789; -.
DR Proteomes; UP000054281; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..474
FT /note="Peptidase M20 dimerisation domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007156098"
FT DOMAIN 223..368
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 474 AA; 50564 MW; C00B691C9A59B9E4 CRC64;
MKLAGKYAHT AFFGAAILGA ACLGALPIAA KDHTAAEAQV LELSKQAIAL RSVRGEGNQT
PQVAALFRDA LLAGGWAAGD IEIVPVGDTA YLIATWAGSD PSLGPIVISA HMDVVEAKPE
DWERDPFIPV VENGYLFGRG ASDTKFDAVQ AMVSVIELRK QGYKPKRSIV IAYSGDEETT
MITAKIIADR LRGARLVLNV DGGSGTLDEK TGKPAYWSWQ GAEKTYGDFQ LEVTNPGGHS
STPRDENAIA QLSAALERIG AYRFKPELND ITRDYFSKAA DFESDPLTSQ AMRAFAADPA
NKAAIAVLRA DPAMIGKIGT TCVPTMVEGG HALNALPQRA TAIVNCRIFP GHPKAEIRAE
LERVAAQPGL TITEINPEYV VDAPASPFDR EFVDAATRAV HAAFGEIPVI ASQASGASDS
MWYRALGVPS YGASGTFSKS SDDYSHGLNE RVPLDNVGRA ITYYHALLKE LTSR
//
