FTSH_NEORI
ID FTSH_NEORI Reviewed; 636 AA.
AC C6V4R9;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=NRI_0402;
OS Neorickettsia risticii (strain Illinois).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=434131;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Illinois;
RX PubMed=19661282; DOI=10.1093/nar/gkp642;
RA Lin M., Zhang C., Gibson K., Rikihisa Y.;
RT "Analysis of complete genome sequence of Neorickettsia risticii: causative
RT agent of Potomac horse fever.";
RL Nucleic Acids Res. 37:6076-6091(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 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; CP001431; ACT69330.1; -; Genomic_DNA.
DR RefSeq; WP_015816219.1; NC_013009.1.
DR AlphaFoldDB; C6V4R9; -.
DR SMR; C6V4R9; -.
DR STRING; 434131.NRI_0402; -.
DR EnsemblBacteria; ACT69330; ACT69330; NRI_0402.
DR KEGG; nri:NRI_0402; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_5; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000001627; 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 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"
FT /id="PRO_0000400364"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 34..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 126..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 497
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; 70267 MW; 15E9679F36C07188 CRC64;
MKKLLENLSL WMGIIILVTL LFGQVALNFG FGIRNEKIQF SEFLDLVEKG EVQKIVIEGY
DISGVLKSGT RFYTKATQYT ELIPLLRKNN VDFQVASGDS FLGLLFNILI SWFPMLLLIG
VWIFFMKQMQ AGGNKTMTFG KSKARLLSDR SNKVTFHDVA GIDEAKEELA EIVEFLREPK
KFQKLGGKIP KGCLLIGPPG TGKTLLAKAI AGEAKVPFFS ISGSDFVEMF VGVGASRVRD
MFEQGKKNAP CLIFIDEIDA VGRHRGVGFG GGNDEREQTL NQLLVEMDGF EANEGVIIIA
ATNRPDVLDP ALLRPGRFDR QITISIPDIA GRQKILEVHL KKIPTAPNVE VSIIARGTPG
FSGADLANLV NESALIAARR NKKVVTNEDF EYARDKILMG MERKSLVMRE EEKLLTAYHE
AGHAVTSLKL EASDPIHKAT IIPRGRALGL VMRLPEHDRV SFTRAKMHAD LIVAMGGRAA
EQVIFGDDKT TSGAASDIKQ ATHLARSMVT KWGMSEKVGP LLYGEQNDPN NHILSIEMSN
LIDSEVKQLI TDALKEATKI LNENIESLHR IAKALLEYET LTGQELSDLL EGKPFLKKTA
DDKKVVSKSS LDVEDDTVDK ETLEKLESDL DTGDKE
