(data stored in ACNUC7421 zone)

HOGENOM: ACEP3_1_PE2554

ID   ACEP3_1_PE2554                       STANDARD;      PRT;   645 AA.
AC   ACEP3_1_PE2554; C7JGX8;
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 -;
DE   (ACEP3_1.PE2554).
GN   Name=ftsH; OrderedLocusNames=APA01_26160;
OS   ACETOBACTER PASTEURIANUS IFO 3283-01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACEP3_1.PE2554.
CC       Acetobacter pasteurianus IFO 3283-01, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7JGX8_ACEP3
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: HOG000217276 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C7JGX8; -.
DR   EMBL; AP011121; BAI00713.1; -; Genomic_DNA.
DR   RefSeq; YP_003189092.1; NC_013209.1.
DR   ProteinModelPortal; C7JGX8; -.
DR   STRING; C7JGX8; -.
DR   GeneID; 8436432; -.
DR   GenomeReviews; AP011121_GR; APA01_26160.
DR   KEGG; apt:APA01_26160; -.
DR   OMA; KPNRESA; -.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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; ACEP3_1.PE2554; -.
KW   cell division ATP-dependent metalloprotease FtsH;
KW   ATP-binding; Cell division; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Protease; Transmembrane;
KW   Transmembrane helix; Zinc.
SQ   SEQUENCE   645 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNNLGRNLAL WVSIILLLLL LVNMFQPGST QHAAQQLAYS DFIADVDTGH VRSVVMQNHN
     ISGTLTDGTA FETYAPLDPS LVTRMVGKGV EVVAKPLEQE GSPLLRYFLN SLPIILLVAA
     WLFMMRQMQG AGGRAMGFGK SRAKMLTEKH GRVTFDDVAG IDEAKGELQE IVDFLKDPQK
     FTRLGGKIPK GVLLVGPPGT GKTLLARAIA GEANVPFFTI SGSDFVEMFV GVGASRVRDM
     FEQGKKAAPC IIFIDEIDAV GRHRGAGMGG GNDEREQTLN QMLVEMDGFE SNEGVILIAA
     TNRPDVLDPA LLRPGRFDRQ VVVPNPDVSG REKILRVHMR KVPLASDVDP RIIARGTPGF
     SGADLANLVN EAALSAARLG RRTVSMREFE DAKDKVLMGV ERRSLIMSDD EKRRTAYHEA
     GHAITAVLVP ESEPIHKATI VPRGRALGMV MRLPEDDRLS MSKKNAFAHL VVAMGGRVAE
     EVIYGKDNVC NGAMGDIKMA TRVARSMVTE WGMSDKLGMI AYADDDQNGG FFAGASRNFS
     EETAREIDEE VRRLVDEAYV QARNYLHDHI DELRRLAEAL LEYETLSGEE IRQIMRGQPI
     ERKEEEESGP VNRRSSVPQV GGPDVQGSDK PENGTGGPVP VPQPS
//

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