(data stored in ACNUC7421 zone)

SWISSPROT: Y638_RHILO

ID   Y638_RHILO              Reviewed;         367 AA.
AC   Q98MC1;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=Putative zinc metalloprotease mll0638;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=mll0638;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB48192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000012; BAB48192.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q98MC1; -.
DR   STRING; 266835.14021580; -.
DR   MEROPS; M50.004; -.
DR   EnsemblBacteria; BAB48192; BAB48192; BAB48192.
DR   KEGG; mlo:mll0638; -.
DR   eggNOG; ENOG4105DZP; Bacteria.
DR   eggNOG; COG0750; LUCA.
DR   HOGENOM; HOG000006282; -.
DR   KO; K11749; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q98MC1.
DR   SWISS-2DPAGE; Q98MC1.
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..367
FT                   /note="Putative zinc metalloprotease mll0638"
FT                   /id="PRO_0000088455"
FT   TRANSMEM        108..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          121..196
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           20
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   METAL           24
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   367 AA;  39923 MW;  0E77DF0CB96D5152 CRC64;
     MFLGTLVPFL FVLTVVVFVH EMGHYLVGRW CGIGVRAFSI GFGPELIGFN DRHGTRWKLC
     AIPLGGYVKF VGDMNATSSQ PTSEELETLT DEERKVAFHT QAIWKRAATV VAGPLFNFLL
     TIVVFSVLFA SYGRYVAEPM VAEVTADSPA AKAGIQPGDR FVSVDGSKVE TFGDVQRLVS
     GRAGDTITFV MLRDGKEVTV TATPQLMEQQ DALGNKVKVA VIGVVNNKEL GQPRLITYTP
     VGAVAAAVEE TGHVIQRTGQ FLQRFAVGRE DKCQLGGPVK IADMAGKAAK LGFEWLVQLV
     ALLSVGIGFL NLLPIPPLDG GHLLFYGVEA VIRRPVSERM MEMAYRAGLL LVLCFMGFVF
     WNDLFGC
//

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