ID FTSH_HELPY Reviewed; 632 AA.
AC P71408; O07679; Q48268;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 27-MAR-2024, entry version 155.
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=HP_1069;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=8892813; DOI=10.1128/jb.178.21.6151-6157.1996;
RA Ge Z., Taylor D.E.;
RT "Sequencing, expression, and genetic characterization of the Helicobacter
RT pylori ftsH gene encoding a protein homologous to members of a novel
RT putative ATPase family.";
RL J. Bacteriol. 178:6151-6157(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9244252; DOI=10.1128/jb.179.15.4676-4683.1997;
RA Beier D., Spohn G., Rappuoli R., Scarlato V.;
RT "Identification and characterization of an operon of Helicobacter pylori
RT that is involved in motility and stress adaptation.";
RL J. Bacteriol. 179:4676-4683(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-632.
RC STRAIN=69A;
RX PubMed=8550601; DOI=10.1074/jbc.271.1.446;
RA Melchers K., Weitzenegger T., Buhmann A., Steinhilber W., Sachs G.,
RA Schaefer K.P.;
RT "Cloning and membrane topology of a P type ATPase from Helicobacter
RT pylori.";
RL J. Biol. Chem. 271:446-457(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 160-419 NUCLEOTIDE-FREE AND
RP COMPLEXED WITH ADP.
RX PubMed=18421140; DOI=10.1107/s090904950706846x;
RA Kim S.H., Kang G.B., Song H.E., Park S.J., Bea M.H., Eom S.H.;
RT "Structural studies on Helicobacter pylori ATP-dependent protease, FtsH.";
RL J. Synchrotron Radiat. 15:208-210(2008).
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 Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:8892813};
CC Multi-pass membrane protein {ECO:0000305|PubMed:8892813}; Cytoplasmic
CC side {ECO:0000305|PubMed:8892813}.
CC -!- DISRUPTION PHENOTYPE: A homozygous disruption strain was not
CC identified, suggesting this gene may be essential.
CC {ECO:0000269|PubMed:8892813}.
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; U59452; AAC44563.1; -; Genomic_DNA.
DR EMBL; U97567; AAB66377.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08115.1; -; Genomic_DNA.
DR EMBL; U59625; AAB05472.1; -; Genomic_DNA.
DR PIR; E64653; E64653.
DR RefSeq; NP_207860.1; NC_000915.1.
DR RefSeq; WP_000805281.1; NC_018939.1.
DR PDB; 2R62; X-ray; 3.30 A; A/B=160-419.
DR PDB; 2R65; X-ray; 3.30 A; A/B/C/D/E=160-419.
DR PDBsum; 2R62; -.
DR PDBsum; 2R65; -.
DR AlphaFoldDB; P71408; -.
DR SMR; P71408; -.
DR DIP; DIP-3549N; -.
DR IntAct; P71408; 4.
DR MINT; P71408; -.
DR STRING; 85962.HP_1069; -.
DR PaxDb; 85962-C694_05525; -.
DR EnsemblBacteria; AAD08115; AAD08115; HP_1069.
DR KEGG; hpy:HP_1069; -.
DR PATRIC; fig|85962.47.peg.1148; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; P71408; -.
DR OrthoDB; 9809379at2; -.
DR PhylomeDB; P71408; -.
DR EvolutionaryTrace; P71408; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..632
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084636"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 31..116
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 138..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 213..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT CONFLICT 275
FT /note="G -> P (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 283..284
FT /note="VV -> MI (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> F (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="H -> D (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..367
FT /note="LQ -> FE (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="RQ -> KL (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> K (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="I -> M (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="A -> G (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="S -> Y (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="V -> F (in Ref. 2; AAB66377)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="K -> E (in Ref. 1; AAC44563 and 4; AAB05472)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="V -> A (in Ref. 1; AAC44563)"
FT /evidence="ECO:0000305"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2R65"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2R62"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2R65"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:2R65"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:2R62"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2R65"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2R62"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2R65"
FT TURN 294..302
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2R65"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2R65"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2R62"
FT TURN 366..370
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2R62"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:2R62"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2R65"
SQ SEQUENCE 632 AA; 69745 MW; 1D0674163FFC206D CRC64;
MKPTNEPKKP FFQSPIILAV LGGILLIFFL RSFNSDGSFS DNFLASSTKN VSYHEIKQLI
SNNEVENVSI GQTLIKASHK EGNNRVIYIA KRVPDLTLVP LLDEKKINYS GFSESNFFTD
MLGWLMPILV ILGLWMFMAN RMQKNMGGGI FGMGSAKKLI NAEKPNVRFN DMAGNEEAKE
EVVEIVDFLK YPERYANLGA KIPKGVLLVG PPGTGKTLLA KAVAGEAHVP FFSMGGSSFI
EMFVGLGASR VRDLFETAKK QAPSIIFIDE IDAIGKSRAA GGVVSGNDER EQTLNQLLAE
MDGFGSENAP VIVLAATNRP EILDPALMRP GRFDRQVLVD KPDFNGRVEI LKVHIKGVKL
ANDVNLQEVA KLTAGLAGAD LANIINEAAL LAGRNNQKEV RQQHLKEAVE RGIAGLEKKS
RRISPKEKKI VAYHESGHAV ISEMTKGSAR VNKVSIIPRG MAALGYTLNT PEENKYLMQK
HELIAEIDVL LGGRAAEDVF LEEISTGASN DLERATDIIK GMVSYYGMSS VSGLMVLEKQ
RNAFLGGGYG SSREFSEKTA EEMDLFIKNL LEERYKHVKQ TLSDYREAIE IMVKELFDKE
VITGERVREI ISEYEVANNL ESRLIPLEEQ AS
//
