FTSH_BUCAP
ID FTSH_BUCAP Reviewed; 613 AA.
AC Q8K9G8;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; Synonyms=hflB;
GN OrderedLocusNames=BUsg_369;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67921.1; -; Genomic_DNA.
DR RefSeq; WP_011053888.1; NC_004061.1.
DR AlphaFoldDB; Q8K9G8; -.
DR SMR; Q8K9G8; -.
DR STRING; 198804.BUsg_369; -.
DR MEROPS; M41.001; -.
DR PRIDE; Q8K9G8; -.
DR EnsemblBacteria; AAM67921; AAM67921; BUsg_369.
DR KEGG; bas:BUsg_369; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_6; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000000416; 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..613
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084629"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 26..98
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 120..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 415
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 613 AA; 68468 MW; 11B4407546F7799C CRC64;
MVKNLIFWLV ITVVLMSVFQ NFNSSDTSNH RVDYSTFLSE VNQDQVREAY INGRIISVTK
KDSSKYITYI PINDPKLLDN LLTKNVKIVG EIPEEPSLLI SIFISWFPML LLIGVWIFFM
RQMQMGGGKG AMSFGKSKAR MLSEDQIQTT FADVAGCDEA KEEVSELVEY LKEPSRFQKL
GGKIPKGILM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEHA
RKSAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFDGNEG VILIAATNRP
DVLDPALLRP GRFDRQVIVA LPDVRGRKQI LKVHMRKVPL SEDVDPMIIA RGTPGFSGAD
LANLVNEAAL FAARFNNRVV SMIHFEKAKD KIMMGSERRS MVMSDFQKES TAYHEAGHVI
IGRLVPDHDP AHKVTIIPRG QALGITFFLP ESDILSISRQ KLESQISTLY GGRLAEEIIY
GSQNVSTGAF NDIKVATNLA RNMVTQWGFS DKLGPLLYAE EEGEVFLGRS VAKAKHMSDE
TARIIDEEVK LLIEVNYNRA RKILNENLDI LHAMKDALIK YETIDSLQID DLMERREVRK
PKGWLEVDQK KDI
