(data stored in SCRATCH 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   11-DEC-2019, entry version 27.
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;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72922.1};
RN   [1] {ECO:0000313|EMBL:ADP72922.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72922.1};
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., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   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 metallopeptidase for
CC       both cytoplasmic and membrane proteins. Plays a role in the quality
CC       control of integral membrane proteins. {ECO:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC       Cytoplasmic side {ECO:0000256|HAMAP-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 M41
CC       family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC       {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; DRQIYVD; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; GSP581103:G1GOQ-79-MONOMER; -.
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   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458, 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, 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
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          194..333
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         202..209
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   REGION          605..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..623
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           424
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           428
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           500
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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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