(data stored in ACNUC7421 zone)

HOGENOM: ACHXA_1_PE4924

ID   ACHXA_1_PE4924                       STANDARD;      PRT;   628 AA.
AC   ACHXA_1_PE4924; E3HNU7;
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   (ACHXA_1.PE4924).
GN   Name=ftsH; OrderedLocusNames=AXYL_04979;
OS   ACHROMOBACTER XYLOSOXIDANS A8.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHXA_1.PE4924.
CC       Achromobacter xylosoxidans A8 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E3HNU7_ACHXA
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 membrane; Multi-pass membrane protein;
CC       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; E3HNU7; -.
DR   EMBL; CP002287; ADP18286.1; -; Genomic_DNA.
DR   RefSeq; YP_003981001.1; NC_014640.1.
DR   GeneID; 9899311; -.
DR   GenomeReviews; CP002287_GR; AXYL_04979.
DR   KEGG; axy:AXYL_04979; -.
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; ACHXA_1.PE4924; -.
KW   cell division protease FtsH;
KW   ATP-binding; Cell division; Cell membrane; Complete proteome;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Nucleotide-binding; Protease; Transmembrane; Transmembrane helix;
KW   Zinc.
SQ   SEQUENCE   628 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNNSFSKVAV WMVIALVLFT VFKQFDGRAQ TQDGVTYTQF MDDAKAGRIR KVDVQGDVLY
     VTPDAGRAYT LTSPGDLWMV SDLLKYGVQV SGKPREEQSL LMSIFVSWFP MLLLIGVWVF
     FMRQMQGGGK GGAFSFGKSR ARMLDENTNQ ITFADVAGCD EAKEDVQELV DFLRDPSKFQ
     KLGGRIPRGV LMVGSPGTGK TLLAKAIAGE AKVPFFSISG SDFVEMFVGV GAARVRDMFE
     NAKKHAPCII FIDEIDAVGR QRGAGLGGGN DEREQTLNQM LVEMDGFESG QGVIVIAATN
     RPDVLDPALL RPGRFDRQVV VPLPDIRGRE QILKVHMRKV PLSPNVDATV LARGTPGFSG
     ADLANLVNEA ALFAARRNGR TVDMSDFEKA KDKIIMGAER RSIVMPEEER KNTAYHESGH
     AIVARLLPKT DPVHKVTIIP RGRALGVTMQ LPETDRYSMD KGRLLSTIAV LFGGRIAEEI
     FMDQMTTGAS NDFERATAIA RDIVTRYGMT DELGPMVYAE NEGEVFLGRS VTKTTHMSEA
     TMQKVDTEIR RIIDEQYSVA RKILEDNRDK VEVMTSALLE WETIDADQIN DIIEGRPPRP
     PKTPQGPSDT SDTPPTGLAA GGNTAAAV
//

If you have problems or comments...

PBIL Back to PBIL home page