Y855_MYCLE
ID Y855_MYCLE Reviewed; 445 AA.
AC O32965; Q9CCF7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Uncharacterized zinc protease ML0855;
DE EC=3.4.24.-;
GN OrderedLocusNames=ML0855; ORFNames=MLCB22.26c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC31236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z98741; CAB11391.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31236.1; ALT_INIT; Genomic_DNA.
DR PIR; A87016; A87016.
DR PIR; T44899; T44899.
DR RefSeq; WP_010907968.1; NC_002677.1.
DR AlphaFoldDB; O32965; -.
DR SMR; O32965; -.
DR STRING; 272631.ML0855; -.
DR EnsemblBacteria; CAC31236; CAC31236; CAC31236.
DR KEGG; mle:ML0855; -.
DR Leproma; ML0855; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_3_11; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..445
FT /note="Uncharacterized zinc protease ML0855"
FT /id="PRO_0000074421"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 445 AA; 48156 MW; 9ADA04E5F31D33D8 CRC64;
MRRSKQGAEG KAEKKAARSA GVCRTTLPGG LRVVTEHLPA VRSASVGVWV GVGSRDEGAT
VAGAAHFLEH LLFKSTSTRT AMDIAQAIDA VGGELNAFTA KEHTCYYAHV LDSDLELAVD
LVADVVLNGR CAVDDVELER DVVLEEIAMR DDDPEDALGD MFLAALFGDH PVGRPVIGTM
ESVSAMTRTQ LHSFHVRRYT PERMVVAVAG NVDHDEMVAL VREHFGSRLI RGRQSAPPRK
STGRINGGPA LTLGKRDAEQ THVLLGVRTP GRSWEHRWAL SVLHTALGGG LSSRLFQEIR
ETRGLAYSVY SALDIFADSG ALSVYAACLP GRFADVMQVI SEVLASVAGD GITEAECRIA
KGSLRGGIIL GLEDSNSWMS RLGRSELNYG KYRGIEHTLQ QIDEVTVEQV NALAHQLLNK
RYGAAVLGPY ASKKTLPRQL RIMVN