(data stored in ACNUC7421 zone)

HOGENOM: ACIAC_1_PE2571

ID   ACIAC_1_PE2571                       STANDARD;      PRT;   641 AA.
AC   ACIAC_1_PE2571; A1TQF1;
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   (ACIAC_1.PE2571).
GN   Name=ftsH; OrderedLocusNames=Aave_2617;
OS   ACIDOVORAX CITRULLI AAC00-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAC_1.PE2571.
CC       Acidovorax avenae subsp. citrulli AAC00-1, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1TQF1_ACIAC
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; A1TQF1; -.
DR   EMBL; CP000512; ABM33189.1; -; Genomic_DNA.
DR   RefSeq; YP_970963.1; NC_008752.1.
DR   ProteinModelPortal; A1TQF1; -.
DR   SMR; A1TQF1; 150-404.
DR   STRING; A1TQF1; -.
DR   MEROPS; M41.001; -.
DR   GeneID; 4667230; -.
DR   GenomeReviews; CP000512_GR; Aave_2617.
DR   KEGG; aav:Aave_2617; -.
DR   NMPDR; fig|397945.5.peg.2244; -.
DR   eggNOG; COG0465; -.
DR   OMA; VHARNVP; -.
DR   PhylomeDB; A1TQF1; -.
DR   ProtClustDB; CLSK951380; -.
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; ACIAC_1.PE2571; -.
KW   FtsH peptidase;
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Nucleotide-binding; Protease; Transmembrane; Transmembrane helix;
KW   Zinc.
SQ   SEQUENCE   641 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNNQWFSKIA VWLVIAMVLF TVFKQFDTRA GASAGNIGYS EFLEEVRGGR IKNATIQEGQ
     GGTEIVATTN DDRKVRTTAT YLDRGLVGDL INNNVKFDVK PREEGSLLMT LLVSWGPMLL
     LIGVWVYFMR QMQGGGKGGA FSFGKSKARM LDENNNTVTF ADVAGCDEAK EEVKEVVDFL
     KDPQKFQKLG GRIPRGLLLV GPPGTGKTLL AKSIAGEAKV PFFSISGSDF VEMFVGVGAA
     RVRDMFENAK KNAPCIIFID EIDAVGRQRG AGLGGGNDER EQTLNQMLVE MDGFETNLGV
     IVVAATNRPD ILDAALLRPG RFDRQVYVTL PDIRGREQIL NVHMRKVPVG QDVNAAVIAR
     GTPGMSGADL ANLCNEAALM AARRNARTVE MQDFEKAKDK IIMGPERKSM VMPEEERRNT
     AYHEAGHALI GKLLPKCDPV HKVTIIPRGR ALGVTMSLPE KDRYSYDREY MLNQISMLFG
     GRIAEEVFMN QMTTGASNDF ERATSIARDM VTRYGMTEAL GPMVYAENEG EVFLGRSVTK
     TNNMSEQTME KVDGEVRRII DEQYALARKL IEDNQDKMHA MANALLEWET IDTEQLDDIM
     AGKPPRPPKD WTPRTPSSGG DNSSGGGTPA PVSSDPSPTV A
//

If you have problems or comments...

PBIL Back to PBIL home page