FTSH_OENOE
ID FTSH_OENOE Reviewed; 715 AA.
AC Q83XX3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
OS Oenococcus oeni (Leuconostoc oenos).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=1247;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=IOEB 8406;
RX PubMed=12732516; DOI=10.1128/aem.69.5.2512-2520.2003;
RA Bourdineaud J.P., Nehme B., Tesse S., Lonvaud-Funel A.;
RT "The ftsH gene of the wine bacterium Oenococcus oeni is involved in
RT protection against environmental stress.";
RL Appl. Environ. Microbiol. 69:2512-2520(2003).
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 -!- FUNCTION: Can complement an E.coli ftsH disruption mutant.
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 -!- INDUCTION: Induced by heat shock (37 degrees Celsius) and osmotic shock
CC (0.5 M NaCl) but not by exposure to alcohol, sulfite or ethidium
CC bromide. {ECO:0000269|PubMed:12732516}.
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; AY196466; AAO43575.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83XX3; -.
DR SMR; Q83XX3; -.
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; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Stress response;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..715
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400366"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 32..137
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 159..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 167..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 715 AA; 78069 MW; 408E7B5CB3F7CFB4 CRC64;
MKNKNRGFFR SSLSYAFVIL AVIFLIYSFF GRSDGSVKHL STTTFLKELK NNKIKDFTIQ
PGDSGVYTIA GDFKKAQKSS SSSSSTTTLL SGYQSSVTKF TAYVLPNNSS LKQITTAAQK
AGVAVNPKPA ASNFWGSMLT LILPTLIMFA LLYWMLIGSQ RGQGGSGGPG GIMSFGRSKA
KPADPKQNKI RFADVAGEEE EKQELVEVVE FLKDPKKFTK LGARIPKGVL LEGPPGTGKT
LLAKAVAGEA KTPFFSISGS DFVEMFVGVG ASRVRDLFEN AKKSAPSIIF IDEIDAVGRR
RGAGMGGGND EREQTLNQIL IEMDGFEGSE GVIVLASTNR SDVLDPALLR SGRFDRKILV
GAPDVKGREA ILRVHAKNKP LAADVDLKVI AQQTPGFVGA DLENLLNEAA LLAARNDEKA
VTAADIDEAE DRVIAGPAKK DRKTTQDERE TVAYHEAGHA IVGLVLNDAQ VVRKVTIVPR
GRAGGYALMM PKDERYLMSE KDAKEELAGL MGGRAAEILI NHVASSGASN DFQQATQIAR
EMVTQYGMSD KLGMVQLEGS SNVFVGDPNN PNPPYSQKTS ELIDEEVRRL TNEAYKRAVD
IIKSHPKQHK AIAEALLKYE TLDEAQIRSL FETGEIPSDL VKDSQRPARP LSYEESKAAL
KKNGAVDNKE AEDELKRTKM IRKMKMIPSR VPIQLQKRRQ PRRLQLLDAV NNKFD
