(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHM1_GEOS0

ID   A0A0F6BHM1_GEOS0        Unreviewed;       634 AA.
AC   A0A0F6BHM1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN   Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   OrderedLocusNames=GY4MC1_0066 {ECO:0000313|EMBL:ADP72922.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72922.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72922.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72922.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc
CC       metallopeptidase for both cytoplasmic and membrane proteins. Plays
CC       a role in the quality control of integral membrane proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR   EMBL; CP002293; ADP72922.1; -; Genomic_DNA.
DR   RefSeq; WP_003247472.1; NC_014650.1.
DR   EnsemblBacteria; ADP72922; ADP72922; GY4MC1_0066.
DR   GeneID; 29237312; -.
DR   KEGG; gmc:GY4MC1_0066; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; GSP581103:G1GOQ-79-MONOMER; -.
DR   Proteomes; UP000002034; 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:ATPase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 1.20.58.760; -; 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;
DR   PRODOM; A0A0F6BHM1.
DR   SWISS-2DPAGE; A0A0F6BHM1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ADP72922.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ADP72922.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ADP72922.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   TRANSMEM      9     27       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   TRANSMEM    110    131       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      194    333       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     202    209       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    425    425       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       424    424       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       428    428       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       500    500       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   634 AA;  70880 MW;  1FCD8D0652888184 CRC64;
     MNRIFRNTIF YLLIFLVVIG VVSFFNGSNQ RTEPMTYDAF ITHLENGDVK SFSMKPERGV
     YEIRGQLKSY SEDQYFSTYV MNSDTVLNRI DAAAQRTRVE VMPADETSGW VTFFTSIIPF
     VIILILFFFL LNQAQGGGSR VMNFGKSRAK LYTDDKRKVR FRDVAGADEE KQELVEIVEF
     LKDPRKFVEL GARIPKGVLL VGPPGTGKTL LARAVAGEAG VPFFSISGSD FVEMFVGVGA
     SRVRDLFETA KKNAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQLLV EMDGFSGNEG
     IIIIAATNRP DILDPALLRP GRFDRQITVD RPDVKGREAV LRVHARNKPL DESVDLKTIA
     MRTPGFSGAD LENLLNEAAL VAARRNKKKI DMSDIDEATD RVIAGPAKKS RVISEKERRI
     VAYHEAGHTV IGMVLDDAEM VHKVTIVPRG QAGGYAVMLP KEDRYFMTKP ELMDKITGLL
     GGRVAEEIVF NEVSTGAHND FQRATNIARR MVTEFGMSEK LGPLQFGQPS GQVFLGRDLH
     NEQNYSDKIA YEIDLEIQRI IKECYEKAKN ILTQYRDKLE LIATTLLEVE TLDAEQIKHL
     FEHGTLPNRD ASNGNNDNGD QDSDVKINIQ KKDE
//

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