FTSH_THEMA
ID FTSH_THEMA Reviewed; 610 AA.
AC Q9WZ49;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=TM_0580;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 147-610 WITH BOUND ADP AND ZINC,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF ASP-500.
RX PubMed=16484367; DOI=10.1073/pnas.0600031103;
RA Bieniossek C., Schalch T., Bumann M., Meister M., Meier R., Baumann U.;
RT "The molecular architecture of the metalloprotease FtsH.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3066-3071(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 147-610 OF MUTANT ALA-207 WITHOUT
RP NUCLEOTIDE, SUBUNIT, AND MUTAGENESIS OF GLY-404.
RX PubMed=19955424; DOI=10.1073/pnas.0910708106;
RA Bieniossek C., Niederhauser B., Baumann U.M.;
RT "The crystal structure of apo-FtsH reveals domain movements necessary for
RT substrate unfolding and translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21579-21584(2009).
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:0000255|HAMAP-Rule:MF_01458,
CC ECO:0000269|PubMed:16484367};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458,
CC ECO:0000269|PubMed:16484367};
CC -!- SUBUNIT: The isolated ADP-bound cytosolic domain forms a 6-fold
CC symmetric protease disk and a 2-fold symmetric AAA ATPase ring. In the
CC absence of nucleotide the AAA ATPase ring also forms symmetric
CC hexamers. {ECO:0000269|PubMed:16484367, ECO:0000269|PubMed:19955424}.
CC -!- INTERACTION:
CC Q9WZ49; Q9WZ49: ftsH; NbExp=5; IntAct=EBI-15819194, EBI-15819194;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD35665.1; -; Genomic_DNA.
DR PIR; E72358; E72358.
DR RefSeq; NP_228390.1; NC_000853.1.
DR RefSeq; WP_004081278.1; NZ_CP011107.1.
DR PDB; 2CE7; X-ray; 2.44 A; A/B/C/D/E/F=147-610.
DR PDB; 2CEA; X-ray; 2.75 A; A/B/C/D/E/F=147-610.
DR PDB; 3KDS; X-ray; 2.60 A; E/F/G=147-610.
DR PDB; 4M8A; X-ray; 1.50 A; A/B/C=34-101.
DR PDB; 4Q0F; X-ray; 1.95 A; A/B/C=34-101.
DR PDB; 7TDO; EM; 3.15 A; A/B/C/D/E/F=1-610.
DR PDBsum; 2CE7; -.
DR PDBsum; 2CEA; -.
DR PDBsum; 3KDS; -.
DR PDBsum; 4M8A; -.
DR PDBsum; 4Q0F; -.
DR PDBsum; 7TDO; -.
DR AlphaFoldDB; Q9WZ49; -.
DR SMR; Q9WZ49; -.
DR DIP; DIP-49026N; -.
DR STRING; 243274.THEMA_01765; -.
DR MEROPS; M41.021; -.
DR DNASU; 897649; -.
DR EnsemblBacteria; AAD35665; AAD35665; TM_0580.
DR KEGG; tma:TM0580; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; Q9WZ49; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR BRENDA; 3.4.24.B17; 6331.
DR BRENDA; 3.4.24.B20; 6331.
DR EvolutionaryTrace; Q9WZ49; -.
DR Proteomes; UP000008183; 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:0042802; F:identical protein binding; IPI:IntAct.
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..610
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400412"
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..107
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 129..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458,
FT ECO:0000269|PubMed:16484367"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 204..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16484367"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16484367"
FT MUTAGEN 404
FT /note="G->L: Complete loss of protease activity and of
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:19955424"
FT MUTAGEN 500
FT /note="D->A: Complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:16484367"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:4M8A"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4M8A"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4M8A"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4M8A"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4M8A"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4M8A"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4M8A"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2CE7"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2CE7"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 414..433
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 481..490
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 498..513
FT /evidence="ECO:0007829|PDB:2CE7"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 547..574
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 576..589
FT /evidence="ECO:0007829|PDB:2CE7"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:2CE7"
FT HELIX 594..600
FT /evidence="ECO:0007829|PDB:2CE7"
SQ SEQUENCE 610 AA; 68099 MW; 83F76468C8495DDF CRC64;
MNRSNIWNLL FTILIIVTLF WLARFFYVEN SPVSKLSYTS FVQMVEDERS VVSEVVIRDD
GVLRVYTKDG RVYEVDAPWA VNDSQLIEKL VSKGIKVSGE RSGSSSFWIN VLGTLIPTIL
FIVVWLFIMR SLSGRNNQAF TFTKSRATMY KPSGNKRVTF KDVGGAEEAI EELKEVVEFL
KDPSKFNRIG ARMPKGILLV GPPGTGKTLL ARAVAGEANV PFFHISGSDF VELFVGVGAA
RVRDLFAQAK AHAPCIVFID EIDAVGRHRG AGLGGGHDER EQTLNQLLVE MDGFDSKEGI
IVMAATNRPD ILDPALLRPG RFDKKIVVDP PDMLGRKKIL EIHTRNKPLA EDVNLEIIAK
RTPGFVGADL ENLVNEAALL AAREGRDKIT MKDFEEAIDR VIAGPARKSK LISPKEKRII
AYHEAGHAVV STVVPNGEPV HRISIIPRGY KALGYTLHLP EEDKYLVSRN ELLDKLTALL
GGRAAEEVVF GDVTSGAAND IERATEIARN MVCQLGMSEE LGPLAWGKEE QEVFLGKEIT
RLRNYSEEVA SKIDEEVKKI VTNCYERAKE IIRKYRKQLD NIVEILLEKE TIEGDELRRI
LSEEFEKVVE
