(data stored in ACNUC7421 zone)

HOGENOM: ACEAZ_1_PE110

ID   ACEAZ_1_PE110                        STANDARD;      PRT;   651 AA.
AC   ACEAZ_1_PE110; D9QSX4;
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 -;Flags:
DE   Precursor; (ACEAZ_1.PE110).
GN   Name=ftsH; OrderedLocusNames=Acear_0111;
OS   ACETOHALOBIUM ARABATICUM DSM 5501.
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACEAZ_1.PE110.
CC       Acetohalobium arabaticum DSM 5501 chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D9QSX4_ACEAZ
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: HOG000217277 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D9QSX4; -.
DR   EMBL; CP002105; ADL11662.1; -; Genomic_DNA.
DR   RefSeq; YP_003826727.1; NC_014378.1.
DR   GeneID; 9512101; -.
DR   GenomeReviews; CP002105_GR; Acear_0111.
DR   KEGG; aar:Acear_0111; -.
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; ACEAZ_1.PE110; -.
KW   membrane protease FtsH catalytic subunit;
KW   ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease; Signal;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   651 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKRFSKNIGF YLIIIAIAFL IAQYFISPAP VKADLSYSEF TQLVEAGKID KVTIIGQELV
     KGQVADGKEF EVNIPGTIEK VEQILQNNEV DIETEPEPEP PWWASILGYL LPTILIFGFW
     FFIMQRMQGG GNKMMSFGKN KARRHEEDEK KKVTFDDVAN YEEVKEELVE VVEFLKNPDK
     FSKLGAEIPK GVLLVGPPGT GKTLMARAVA GEAGVPFFII SGSDFVEMFV GVGASRVRDL
     FEQGKENAPC IIFIDELDAV GRQRGAGVGG GHDEREQTLN QLLVEMDGFE ANEGIILMAA
     TNRPDVLDPA LLRPGRFDRQ VLVDKPDFKG RKGVLEIHVQ DKPLTGDVDL DILAKRTPGF
     TGADMENLAN EAAILAARRN KKEISMLEFD DAIDRVLAGP KKKSRIISDK EKDIVSYHET
     GHALLGELLE HADSTHKVSI IPRGRAGGFT VNLPEADKNY VTKSELIDKV TSLLGGRVAE
     EVFLDDISTG AQNDLERATK IVRNMVTDYG MSEEVGPLAL GQKNGDQVFL GRDLSKDKNY
     SEEVASLIDK EVKRFVEEAY DKATRILSGN KEMVEKMVTE LKEEETLVSD DIRRIIAEFK
     DDYEYNPDDE ADEESKKATK NTENTIEKET DDLDSKLDDS TDKKININLT D
//

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