ID   FTSH1_THERP             Reviewed;         652 AA.
AC   B9KXV3;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=trd_0293;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM06215.1; -; Genomic_DNA.
DR   RefSeq; WP_012641703.1; NC_011959.1.
DR   AlphaFoldDB; B9KXV3; -.
DR   SMR; B9KXV3; -.
DR   STRING; 309801.trd_0293; -.
DR   MEROPS; M41.009; -.
DR   EnsemblBacteria; ACM06215; ACM06215; trd_0293.
DR   KEGG; tro:trd_0293; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_0; -.
DR   OMA; QYGMTER; -.
DR   OrthoDB; 190468at2; -.
DR   Proteomes; UP000000447; 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 membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Plasmid; Protease; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..652
FT                   /note="ATP-dependent zinc metalloprotease FtsH 1"
FT                   /id="PRO_0000400410"
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..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        132..652
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          623..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..652
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         429
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   652 AA;  72162 MW;  919876351795C1C4 CRC64;
     MSDNKWLRNG FVWMILIIAA IAVWVTFVQG GRGGATITTQ EMAADIKAGK VERLVMTSGS
     DEIQVQYIGT NEVRTLRLPP NVDIFELLKT FGIDPQQVDI QTHRASQWGN VLGTLTFLLP
     TLFLIGVIIF MMRQAQGTNN QALSFGKSRA RVFTSNRPTV TFDDVAGVDE AKEELQEIVE
     FLKYPEKFAA LGARIPRGVL LVGPPGTGKT LLSRAVAGEA GVPFFSISGS EFVEMFVGVG
     ASRVRDLFDQ AKRNAPCIVF IDEIDAVGRQ RGAGLGGSHD EREQTLNQIL VEMDGFDSST
     NVIVIAATNR PDVLDPALLR PGRFDRQVVL DRPDLHGRLA ILKVHTRGKP LESDVDLEDL
     ARQTPGFSGA DLENLVNEAA ILAARRNKKT IGRRELYEAI DRVVAGPERK SRRISEREKL
     MTAYHEAGHA LVARMLPHAD PVHKVSIVAR GMMGGYTRVL PEEDRFFWTK KQFEAQLAVF
     MAGLVAEELV FQEVSTGAAN DIERATTLAR RMVTEFGMSE RLGPLAFGRK EELVFLGREI
     AEQRNYSDQV AYEIDQEVRR LIDQAYQTAK QILLDHMDKL EKIATLLVEK ETLDGHEIEA
     LFDEPRPRPE LVGPPLTRPA ALIATPETAR PDSPSEARPA APVPHIKPQP AS