FTSH_HELFC
ID FTSH_HELFC Reviewed; 638 AA.
AC O32617; E7A9G4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
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};
GN OrderedLocusNames=Hfelis_12570;
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RX PubMed=9440521; DOI=10.1128/jb.180.2.317-329.1998;
RA Bayle D., Waengler S., Weitzenegger T., Steinhilber W., Volz J.,
RA Przybylski M., Schaefer K.P., Sachs G., Melchers K.;
RT "Properties of the P-type ATPases encoded by the copAP operons of
RT Helicobacter pylori and Helicobacter felis.";
RL J. Bacteriol. 180:317-329(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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: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}.
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DR EMBL; AJ001932; CAA05102.1; -; Genomic_DNA.
DR EMBL; FQ670179; CBY83341.1; -; Genomic_DNA.
DR PIR; T47267; T47267.
DR RefSeq; WP_013469705.1; NC_014810.2.
DR AlphaFoldDB; O32617; -.
DR SMR; O32617; -.
DR STRING; 936155.HFELIS_12570; -.
DR EnsemblBacteria; CBY83341; CBY83341; HFELIS_12570.
DR GeneID; 36133586; -.
DR KEGG; hfe:HFELIS_12570; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_7; -.
DR OMA; QVMQFGQ; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000007934; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
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 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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..638
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084635"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 37..122
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 144..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 441
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 638 AA; 70245 MW; CAA4818021A243A0 CRC64;
MDNNHKGPND PNSKKPLLQN PLLLIAIFGI IIFVAMRVMN SDEGFGDRFL STSTKNISYH
EMKELIEKKE VDSVSIGQTL IKAISKEGNN KTIYVAKRVP DLSLVPLLDS QKINYSGFSE
SNFFADILGW LLPVLVILGL WMFMASRMQK NMGGGIFGMG SSKKLINAEK PKVRFNDMAG
NEEAKEEVVE IVDFLKYPDR YASLGAKIPK GVLLVGPPGT GKTLLAKAVA GEASVPFFSM
GGSSFIEMFV GLGASRVRDL FDIAKKEAPS IIFIDEIDAI GKSRAAGGMI SGNDEREQTL
NQLLAEMDGF GSENAPVIVL AATNRPEILD PALLRPGRFD RQVLVDKPDF KGRVEILKVH
IKPVKLANDV DLQEIAKLTA GLAGADLANI INEAALLAGR NNQKEVKQQH LKEAVERGIA
GLEKKSRRIS PKEKKIVAYH ESGHAVISEM TKGSARVNKV SIIPRGMAAL GYTLNTPEEN
KYLMQKHELI AEIDVLLGGR AAEDVFLQEI STGASNDLER ATDIIKGMVS YYGMSDVSGL
MVLEKQRNSF LGGGFGSGRE FSEKMAEEMD SFIKNLLEER YVHVKQTLSD YKDAIEVMVN
ELFEKEVITG ERVREIISEY EVSHNLQTRL VPLEEHAS
