FTSH_AQUAE
ID FTSH_AQUAE Reviewed; 634 AA.
AC O67077;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=aq_936;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 405-634, COFACTOR, AND SUBUNIT.
RX PubMed=16762831; DOI=10.1016/j.molcel.2006.04.020;
RA Suno R., Niwa H., Tsuchiya D., Zhang X., Yoshida M., Morikawa K.;
RT "Structure of the whole cytosolic region of ATP-dependent protease FtsH.";
RL Mol. Cell 22:575-585(2006).
CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC both cytoplasmic and membrane proteins. Plays a role in the quality
CC control of integral membrane proteins. {ECO:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:16762831};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:16762831};
CC -!- SUBUNIT: The isolated protease domain (residues 405-634) forms a stable
CC hexamer. {ECO:0000269|PubMed:16762831}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein;
CC Cytoplasmic side.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; AE000657; AAC07029.1; -; Genomic_DNA.
DR PIR; B70381; B70381.
DR RefSeq; NP_213640.1; NC_000918.1.
DR RefSeq; WP_010880578.1; NC_000918.1.
DR PDB; 2DI4; X-ray; 2.79 A; A/B=405-634.
DR PDB; 4WW0; X-ray; 2.96 A; A/B/C=141-634.
DR PDB; 4Z8X; X-ray; 3.25 A; A/B/C=142-634.
DR PDB; 6GCN; X-ray; 2.95 A; A/B/C/D=151-608.
DR PDB; 6GCO; X-ray; 3.32 A; A/B=151-608.
DR PDBsum; 2DI4; -.
DR PDBsum; 4WW0; -.
DR PDBsum; 4Z8X; -.
DR PDBsum; 6GCN; -.
DR PDBsum; 6GCO; -.
DR AlphaFoldDB; O67077; -.
DR SMR; O67077; -.
DR STRING; 224324.aq_936; -.
DR MEROPS; M41.021; -.
DR TCDB; 3.A.29.1.4; the mitochondrial inner membrane i-aaa protease complex (mimp) familly.
DR EnsemblBacteria; AAC07029; AAC07029; aq_936.
DR KEGG; aae:aq_936; -.
DR PATRIC; fig|224324.8.peg.734; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR InParanoid; O67077; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR BRENDA; 3.4.24.B17; 396.
DR BRENDA; 3.4.24.B20; 396.
DR EvolutionaryTrace; O67077; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..634
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084625"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 27..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 122..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 615..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:4WW0"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:6GCN"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4Z8X"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4WW0"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4WW0"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 362..378
FT /evidence="ECO:0007829|PDB:6GCN"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 409..428
FT /evidence="ECO:0007829|PDB:2DI4"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4Z8X"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 463..488
FT /evidence="ECO:0007829|PDB:2DI4"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:2DI4"
FT HELIX 494..509
FT /evidence="ECO:0007829|PDB:2DI4"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:2DI4"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:6GCN"
FT HELIX 541..568
FT /evidence="ECO:0007829|PDB:2DI4"
FT HELIX 570..583
FT /evidence="ECO:0007829|PDB:2DI4"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2DI4"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:2DI4"
SQ SEQUENCE 634 AA; 70686 MW; 320D4A6B3F58AA53 CRC64;
MNALKNFFIW AIIIGAAIVA FNLFEGKREF TTKVSLNEVV KLVEEGKVSY AEVRGNTAII
QTKDGQKLEV TLPPNTNLVD KMVEKGVRVE VANPEPPGGW LVNVFLSWLP ILFFIGIWIF
LLRQMSGGGN VNRAFNFGKS RAKVYIEEKP KVTFKDVAGI EEVKEEVKEI IEYLKDPVKF
QKLGGRPPKG VLLYGEPGVG KTLLAKAIAG EAHVPFISVS GSDFVEMFVG VGAARVRDLF
ETAKKHAPCI IFIDEIDAVG RARGAIPVGG GHDEREQTLN QLLVEMDGFD TSDGIIVIAA
TNRPDILDPA LLRPGRFDRQ IFIPKPDVRG RYEILKVHAR NKKLAKDVDL EFVARATPGF
TGADLENLLN EAALLAARKG KEEITMEEIE EALDRITMGL ERKGMTISPK EKEKIAIHEA
GHALMGLVSD DDDKVHKISI IPRGMALGVT QQLPIEDKHI YDKKDLYNKI LVLLGGRAAE
EVFFGKDGIT TGAENDLQRA TDLAYRMVSM WGMSDKVGPI AIRRVANPFL GGMTTAVDTS
PDLLREIDEE VKRIITEQYE KAKAIVEEYK EPLKAVVKKL LEKETITCEE FVEVFKLYGI
ELKDKCKKEE LFDKDRKSEE NKELKSEEVK EEVV
