(data stored in ACNUC29543 zone)

HOGENOM: MARMS_1_PE1008

ID   MARMS_1_PE1008                       STANDARD;      PRT;   659 AA.
AC   MARMS_1_PE1008; A6VU22;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH; EC=3.4.24 -;Flags:
DE   Precursor; (MARMS_1.PE1008).
GN   Name=ftsH; OrderedLocusNames=Mmwyl1_1020;
OS   MARINOMONAS SP. MWYL1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinomonas.
OX   NCBI_TaxID=400668;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MARMS_1.PE1008.
CC       Marinomonas sp. MWYL1 chromosome, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:A6VU22_MARMS
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc
CC       metallopeptidase for both cytoplasmic and membrane proteins. Plays
CC       a role in the quality control of integral membrane proteins (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family.
CC   -!- GENE_FAMILY: HOG000217277 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A6VU22; -.
DR   EMBL; CP000749; ABR69951.1; -; Genomic_DNA.
DR   RefSeq; YP_001339886.1; NC_009654.1.
DR   ProteinModelPortal; A6VU22; -.
DR   SMR; A6VU22; 143-397.
DR   STRING; A6VU22; -.
DR   MEROPS; M41.001; -.
DR   GeneID; 5367458; -.
DR   GenomeReviews; CP000749_GR; Mmwyl1_1020.
DR   KEGG; mmw:Mmwyl1_1020; -.
DR   eggNOG; COG0465; -.
DR   OMA; TYIPVND; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:HAMAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_01458; FtsH; 1; -.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; Pept_M41_FtsH.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   HOGENOMDNA; MARMS_1.PE1008; -.
KW   ATP-dependent metalloprotease FtsH;
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Nucleotide-binding; Protease; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
SQ   SEQUENCE   659 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLKNILLWLV IAAVLLTVFN NFNTTSDTNR ISYSEFVKEV QDGRIAKVVV DGYTISGSRT
     SGDTFDTVRP AAADPKIMDD LLSNNVIVEG RMPEQQSIWT QLLVASFPIL LILAIFMFFM
     RQMQGGGGGK GGPMSFGKSK ARLLPEDQIK TTFADVAGCD EAKEDTSELV DFLREPSKFQ
     RLGGKIPRGI LMCGPPGTGK TLLAKAIAGE AKVPFFTISG SDFVEMFVGV GASRVRDMFE
     QAKKHAPCII FIDEIDAVGR NRGSGMGGGN DEREQTLNQL LVEMDGFEGN EGIIVIAATN
     RPDVLDPALL RPGRFDRQVQ VGLPDIRGRE QILKVHLRKV PCDDDVEPKN IARGTPGFSG
     ADLANLVNEA ALFAARSNRR LVNMEQLELA KDKILMGAER KTMVMSDKEK LNTAYHEAGH
     TIIGYLMPEH DPVYKVSIIP RGRALGVTMY LPEEDKYSIS KRGLESQVCS LYGGRIAEEM
     IHGFDGVSTG ASNDIERATS IARNMVTKWG LSEKLGPFAY EEDDNNGGYI SGPTGSKANY
     FSPETGKIID AEVQDIITRC YAKATHILEE NRSKLDVMAE ALMQYETIDA KQIKEIMDGK
     KPSAPEGWSD PSANTPKGGA NQEIDEVDAT SDVSASENGT DSENVDSNSG QTSPKPAGE
//

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