FTSH_PSELT
ID FTSH_PSELT Reviewed; 626 AA.
AC A8F7F7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Tlet_1535;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) 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; CP000812; ABV34091.1; -; Genomic_DNA.
DR RefSeq; WP_012003567.1; NC_009828.1.
DR AlphaFoldDB; A8F7F7; -.
DR SMR; A8F7F7; -.
DR STRING; 416591.Tlet_1535; -.
DR MEROPS; M41.021; -.
DR EnsemblBacteria; ABV34091; ABV34091; Tlet_1535.
DR KEGG; tle:Tlet_1535; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR OMA; YDKQGGG; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000002016; 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 Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..626
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400411"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 29..108
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 130..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 626 AA; 70073 MW; 1DDC2BA3D0096815 CRC64;
MNGNRPNYIS LIFAALVILS LFWLVRSFYF DTSAPSKMSF SDFIQMAYEE PTRIAEVVVR
DDGILRVTTK RGEYYEIYAP WFMQDSETIK VLSEKGVRVT GEKGVSSSFW VNVIGNVIFI
GFLLFMFFFM MRTISGRNNQ AFTFTKSRAQ MNRPGQARVT FKDVAGVDEA VEELKETVLF
LKDPGRFSKI GARMPKGILL VGPPGTGKTL LARAVAGEAN VPFFHISGSD FVELFVGVGA
ARVRDLFNQA KANAPCIVFI DEIDAVGRHR GAGLGGGHDE REQTLNQLLV EMDGFDVRQG
IVVMAATNRP DILDPALLRP GRFDKKVVLD TPDVRGREEI LKIHARNKPI AEDVDIRVLA
QRTTGFVGAD LENLVNEAAL LAARNGRDKI KMEDFEEAID RVIAGPARKS RVISPREKRI
VAYHEVGHAI VSSLLPNADP VHRISIIPRG YRALGYTLQL PAEDRYLVTK QELLDQITGL
LGGRAAEELI FQEVTTGAAS DIERATELAR RMVCQFGMSD KLGPLSWGKT EQEIFLGKEL
TRMRNYSEEV ASEIDEEVRK IVTESYDRAK EILTKYHKQL DELVELLLER EVLEGEELRK
ILKTELGEEM VNHDKLRAAA GSEQDS
