(data stored in SCRATCH zone)

SWISSPROT: E3J7B9_FRAIE

ID   E3J7B9_FRAIE            Unreviewed;       718 AA.
AC   E3J7B9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 51.
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=FraEuI1c_0306 {ECO:0000313|EMBL:ADP78392.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78392.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78392.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
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., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR   EMBL; CP002299; ADP78392.1; -; Genomic_DNA.
DR   RefSeq; WP_013421515.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0306; -.
DR   MEROPS; M41.015; -.
DR   EnsemblBacteria; ADP78392; ADP78392; FraEuI1c_0306.
DR   KEGG; fri:FraEuI1c_0306; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; FSP298654:G1GOT-306-MONOMER; -.
DR   Proteomes; UP000002484; 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; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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; E3J7B9.
DR   SWISS-2DPAGE; E3J7B9.
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:UP000002484};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ADP78392.1};
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:ADP78392.1};
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:ADP78392.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
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    105    126       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      190    329       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     198    205       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    421    421       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       420    420       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       424    424       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       496    496       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   718 AA;  77296 MW;  B286FA87DD76A9D1 CRC64;
     MTPRRIFRGW VVLALLVLLV IFLTTNVLSG PKEYSKENLH DIQAKIAAGQ VKSATIEDSK
     QIVQITTKDD KKYESSYVTN QAVSLAAELN DKNVPYEVKV ERSNVLVSLL LNLLPLVLVV
     ALFLFLMNQM QGGGNRVMNF GKSKAKLVNK DTPKTTFADV AGADEALEEL QEIKEFLENP
     GKFQAIGAKI PKGVLLYGPP GTGKTLLARA VAGEAGVPFY SISGSDFVEM FVGVGASRVR
     DLFEQAKANA PAIIFVDEID AVGRHRGAGL GGGHDEREQT LNQLLVEMDG FDVKGGVILI
     AATNRPDILD PALLRPGRFD RQIVVDRPDL LGREAILKVH AKGKPIGPDV DLLVIARRTP
     GFTGADLANV LNEAALLAAR ADQKMISSDL LEESIDRVLA GPERKTRAMS DKEKKRIAYH
     EGGHALVAHA LPNSDPVHKI TILPRGRALG YTMQLPLEDK YLSTRSEMLD KLAVLLGGRT
     AEEVVFHEPT TGASDDIEKA TQIARAMVTQ YGMSDKLGAL KFGAESGEVF LGREVGHQRD
     YSEAVAGEID NEVRKLIEAA HDEAWEVLNT YRDELDNLVL RLMDTETLSK DDVLETFATV
     QKRPVRGFYT GVGRRVPSDR PPVQTPAELG LVASDVADLV KGNGNGNGHP TGNGSPGLNN
     PAAAPGQGAD TGHGPVSGPV NGPTGPAGPP AAPPPDAPRI SNPWAPPVWP NDDERKRS
//

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