(data stored in ACNUC7421 zone)

HOGENOM: ACIAD_1_PE2580

ID   ACIAD_1_PE2580                       STANDARD;      PRT;   631 AA.
AC   ACIAD_1_PE2580; Q6F8N2;
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   (ACIAD_1.PE2580).
GN   Name=ftsH; OrderedLocusNames=ACIAD2853;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE2580.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6F8N2_ACIAD
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; Q6F8N2; -.
DR   EMBL; CR543861; CAG69583.1; -; Genomic_DNA.
DR   RefSeq; YP_047405.1; NC_005966.1.
DR   ProteinModelPortal; Q6F8N2; -.
DR   SMR; Q6F8N2; 146-400.
DR   STRING; Q6F8N2; -.
DR   MEROPS; M41.001; -.
DR   GeneID; 2878828; -.
DR   GenomeReviews; CR543861_GR; ACIAD2853.
DR   KEGG; aci:ACIAD2853; -.
DR   NMPDR; fig|62977.3.peg.2598; -.
DR   eggNOG; COG0465; -.
DR   OMA; KKESTNI; -.
DR   PhylomeDB; Q6F8N2; -.
DR   ProtClustDB; CLSK830697; -.
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; ACIAD_1.PE2580; -.
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   631 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLFKNAVL WLIILGVLIL IFSNISDRNK PAAMNYSEFV ASVNAGQIKQ VTIDGLNISG
     EKTNGSHFET VRPQVEDTEL LPSLNKNKVV VEGTAPQRQG LLMQLLIASF PVLLIILLFM
     FFMRNMGGGA GGKNGPMSFG KSKAKMLSED QIKVTFKDVA GCDEAKQEVV EIVDFLKDPA
     KFKRLGATIP RGVLMVGPPG TGKTLLAKAI AGEAKVPFFS ISGSDFVEMF VGVGASRVRD
     MFEQAKRHAP CIIFIDEIDA VGRHRGSGTG GGHDEREQTL NQMLVEMDGF EGNEGVIVIA
     ATNRVDVLDK ALLRPGRFDR QVMVGLPDIN GREQILNVHL TKLPSVTGVD VKVLARGTPG
     FSGAQLANLV NEAALFAARR NKNTVDMHDF EDAKDKIYMG PERKSMILRE EERRATAYHE
     SGHAIVAEVL PGTDPVHKVT IMPRGWALGV TWQLPEQDQI SHYKDKMLNE ISILFGGRIA
     EEIFINQQST GASNDFERAT KMARAMVTKY GMSDRLGVMV YEDDNTQGFF GNVGSRTISE
     ATQQQVDQEV RRILDEQYKV AWDILEQNKD KAHVMVKALM EWETIDREQV RDIMEGREPR
     PPKVYVAENP VIDVEPPSNG PSTPPPLPSM G
//

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