FTSH1_THEPX
ID FTSH1_THEPX Reviewed; 611 AA.
AC B0K5A3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
GN OrderedLocusNames=Teth514_0793;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
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., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) 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 membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC 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; CP000923; ABY92096.1; -; Genomic_DNA.
DR RefSeq; WP_003867798.1; NC_010320.1.
DR AlphaFoldDB; B0K5A3; -.
DR SMR; B0K5A3; -.
DR MEROPS; M41.021; -.
DR PRIDE; B0K5A3; -.
DR EnsemblBacteria; ABY92096; ABY92096; Teth514_0793.
DR KEGG; tex:Teth514_0793; -.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
DR Proteomes; UP000002155; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..611
FT /note="ATP-dependent zinc metalloprotease FtsH 1"
FT /id="PRO_5000304475"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 28..107
FT /note="Extracellular"
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..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 611 AA; 68035 MW; F98280B5CDA188EC CRC64;
MNDNNKIIRS MVLYLLIFIA IYAMVQLYSQ STEPITDIDY GQLIKYIDAN QVKSITLVGN
DVKGVLKNGT EFKSRVPDVT NFMSFVNPYI LQGKLDFKSE PQVGPPWWVQ MLPSLFLIVI
FIIFWYIFMQ QAQGGGGSKV MSFGKSRARM ITDKDKRVTF NDVAGADEEK EELQEIVEFL
KYPKKFLELG ARIPKGVLLV GPPGTGKTLL AKAVAGEAGV PFFSISGSDF VEMFVGVGAA
RVRDLFDQAK KNAPCIVFID EIDAVGRQRG AGLGGGHDER EQTLNQLLVE MDGFSVNEGI
IVIAATNRPD ILDPALLRPG RFDRHITVGI PDIKGREEIL KIHSRNKPLA PDVSLQVLAR
RTPGFTGADL ENLMNEAALL AARRGLKQIT MAELEEAITR VIAGPEKRSR IMSEKDKKLV
AYHEAGHAVV AKLLPNTPPV HEVTIIPRGR AGGYTMLLPE EDKYYMSKSE MMDEIVHLLG
GRVAESLVLN DISTGAQNDI ERATNIARKM VTEYGMSERL GPMTFGTKSE EVFLGRDLGR
TRNYSEEVAA EIDREIKRII EEAYKRAESL LKENIDKLHR VAKALIEKEK LNGEEFEKVF
NGEDIEGVQF A
