FTSH_TRIEI
ID FTSH_TRIEI Reviewed; 667 AA.
AC Q10ZF7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Tery_3253;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Stromal 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; CP000393; ABG52367.1; -; Genomic_DNA.
DR AlphaFoldDB; Q10ZF7; -.
DR SMR; Q10ZF7; -.
DR STRING; 203124.Tery_3253; -.
DR MEROPS; M41.017; -.
DR PRIDE; Q10ZF7; -.
DR EnsemblBacteria; ABG52367; ABG52367; Tery_3253.
DR KEGG; ter:Tery_3253; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Nucleotide-binding; Protease; Thylakoid; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..667
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400414"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 72..151
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 173..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 465
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 243..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 667 AA; 73570 MW; 29594848D7A0FD9C CRC64;
MKNFGQQIKT DELKGINHHN WSLCQAQSNT QKAKILFGRI PGGKLTRKLG WKILATGIIA
QAVLLVSPAF ANSTQKNLSY SQLLDKIQAG EVTEIDYYPS RGIAKVSLKG QRSREGMYIV
QMFEHVPELL DQVRAQKIDF ELKRSPDNSV AMGIIFNILI VFVVIVVLLA ILRRSSQSQG
NALNFGKSRA RFQMEAKTGV LFEDVAGIEE AKEELQEVVS FLKKPEKFTA IGAKIPKGVL
LVGPPGTGKT LLAKAIAGEA GVPFFSISGS EFVEMFVGVG ASRVRDLFKK AKENAPCIIF
IDEIDAVGRQ RGAGIGGGND EREQTLNQLL TEMDGFEGNS GIIIIAATNR PDVLDVALLR
PGRFDRQVTV DLPAYKGRLG ILEVHARNKK LTPEISLEAI ARKTPGFSGA DLANMLNEAA
ILTARRRKEG ITPNEIDDAI DRVTIGLSLT PLLDGKKKRL IAYHELGHAL LMTLLKNSDL
LNKVTIIPRS GGVGGFAQPI MDEGMIDSGM YTRGWLIDRI TISLGGRAAE EEIFGLAEVT
VGAANDIRSV ASLAREMVTR YGMSDLGPLA LENPNGEVFL GRGWQSQQPE YSEEVAIKID
HQIRTMVFHC YEKARKIIRE NRVLMDRLVD LLIEKETIEG DEFRRIVSEY TELPKKQKSL
INLEKKI
