FTSH1_METI4
ID FTSH1_METI4 Reviewed; 636 AA.
AC B3DV46;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 1 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH1 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=Minf_1144;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(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: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; CP000975; ACD83199.1; -; Genomic_DNA.
DR RefSeq; WP_012463481.1; NC_010794.1.
DR AlphaFoldDB; B3DV46; -.
DR SMR; B3DV46; -.
DR STRING; 481448.Minf_1144; -.
DR MEROPS; M41.021; -.
DR EnsemblBacteria; ACD83199; ACD83199; Minf_1144.
DR KEGG; min:Minf_1144; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR OMA; YDKQGGG; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000009149; 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..636
FT /note="ATP-dependent zinc metalloprotease FtsH 1"
FT /id="PRO_0000400353"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 40..126
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 148..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 636 AA; 70426 MW; BFBBE79695275FF3 CRC64;
MKLSPPKKNL PPQKNNEPPF PYLRLLVQVG IALFLVWIWQ ESLHKATVST IPYSEFLNKI
NQKEIIECKI TPDEIYGKML VSKPEEKGQP PKIALFSTVR VDDPDLVKRL QSAGVVYGSV
KPSLLSQILF SWVVPILIFF LVWFALARFM GGGGAGYSLL NIGKSRARLL VDESTGVTFA
DVAGCDEAKY ELQEVVDFLK NPSRYRALGA KIPKGVLLVG PPGTGKTLLA KAVAGEAKVP
FFSISGSEFV EMFVGVGAAR VRDLFGQAKS KAPCIVFIDE LDAIGRQRGV RIQVGSDEHE
QTLNQLLVEM DGFDPNEGII VLAATNRPEI LDRALLRPGR FDRQVVVDLP DANGREAILR
VHARGKPLSE NIDFKEIAQA TMGFSGADLA NLLNEAALLA ARRKSSRIEQ VDLLEAMEKV
IAGPERKSRV LSEKERERVA YHEVGHALVA FYSEHAEPVR KISIVPRGKS ALGYTLQLPT
AQKYLLSKSE LLDRICVAMG GRAAEELIYG DITTGAENDL EVATTIARQM VCLYGMGEKS
GLAHYVPPQP LLGGLDTSYL KECSDETARI IDLEIEKILE ENYQRALSIL RHHHVELKEV
TKYLLQKETL NAEEFKSILE NLKEQRKEAP SYSSTL
