ID A0A258GUE2_9PROT Unreviewed; 313 AA.
AC A0A258GUE2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Peptidase M15B domain-containing protein {ECO:0000259|Pfam:PF02557};
GN ORFNames=B7Y90_11720 {ECO:0000313|EMBL:OYX47999.1};
OS Alphaproteobacteria bacterium 32-64-14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1970492 {ECO:0000313|EMBL:OYX47999.1, ECO:0000313|Proteomes:UP000215897};
RN [1] {ECO:0000313|EMBL:OYX47999.1, ECO:0000313|Proteomes:UP000215897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-64-14 {ECO:0000313|EMBL:OYX47999.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYX47999.1}.
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DR EMBL; NCEM01000024; OYX47999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258GUE2; -.
DR Proteomes; UP000215897; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14847; DD-carboxypeptidase_like; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..313
FT /note="Peptidase M15B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012446377"
FT DOMAIN 124..267
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
FT REGION 37..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 33607 MW; 90DAA7AE3A2E0729 CRC64;
MKIGRFLVVP AFSAALAAGL AACSASAGPD TADIVTPSSA AQAAAGESLE LASAQPPPDS
IAAEPPPGGT DPAAPEATPP SDAAQPATSH VALKYLIGDV DPATDPKFAR IPDKYIGGSR
VWGHKDAVDA FVRMAEDAAA NGYKLKIVSA FRSFSDQKQI WDDKWNGKTL VGGKKLNTSL
PDPKARALKI LEFSSMPGTS RHHWGTDFDL NALDNKYFTN TKEGRRIYDW LVGHAANYGF
CQVYTAKGEG GRPTGYEEEK WHWSYRPVAA WYLKQYPVDV GYERLTGFAG AETAKAIDVI
PNYVQGINPE CTQ
//