(data stored in ACNUC7421 zone)

HOGENOM: SPITD_1_PE1012

ID   SPITD_1_PE1012                       STANDARD;      PRT;   619 AA.
AC   SPITD_1_PE1012; E0RSK1;
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   (SPITD_1.PE1012).
GN   Name=ftsH; OrderedLocusNames=STHERM_c10430;
OS   SPIROCHAETA THERMOPHILA DSM 6192.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=665571;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SPITD_1.PE1012.
CC       Spirochaeta thermophila DSM 6192 chromosome, complete genome.
CC       nt) ;
CC   -!- ANNOTATIONS ORIGIN:E0RSK1_SPITD
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; E0RSK1; -.
DR   EMBL; CP001698; ADN01988.1; -; Genomic_DNA.
DR   RefSeq; YP_003874261.1; NC_014484.1.
DR   GeneID; 9756297; -.
DR   GenomeReviews; CP001698_GR; STHERM_c10430.
DR   KEGG; sta:STHERM_c10430; -.
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; SPITD_1.PE1012; -.
KW   cell division protease 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   619 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNHERDPKQP QFQFNPNSNR FALIFLFALI TLFIISFFFS SQNTGLEIPY STFLSYLEEG
     RVDSVTILDQ FEIRGTLQSR DGERTLFTTK IPYYDDMLMR ELREKGVRVS GDVKGVSPLR
     IVLELIPWII GFLFIWFMFR QMQVGGNKAF SFGKSRARQY QDGKKVMFAD VAGQEEAKNE
     LQEVVEFLKN PHKFTRMGAR IPKGVLLVGM PGTGKTLLAR AVAGEAGVPF FHMSGSDFVE
     MFVGVGAARV RDLFDQGRKH APCIIFIDEL DAVGRVRGAG YGGGHDEREQ TLNQLLVEMD
     GFESKEGVIV LAATNRPDVL DPALLRPGRF DRQVVVDMPD VKEREAILRI HARKVPLGED
     VDFERVARGT AGTSGADLEN LVNEAALLAA RKNKGVVEME DFEEARDKIL MGVARKSRVL
     SREEKEKTAY HESGHALLHF LLEHVDPLHK VTIVPRGRAL GMAVSLPEKD EYSKSKSWLM
     DRIKVAFGGY AAEKIVYNET TTGAKEDIRQ ATEIARRMVC EWGMSETLGP VALGQEEEPI
     FIGKEIARHK DYSEETARKI DEEIRNILTS ALNEVMNLLG EHKEKLDVLA RTLIERETLT
     EEDICELLNM RPRRVPGEA
//

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