(data stored in ACNUC7421 zone)

SWISSPROT: FTSH_THET1

ID   FTSH_THET1              Reviewed;         646 AA.
AC   D1CDT8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 51.
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};
GN   OrderedLocusNames=Tter_0172;
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1;
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000255|HAMAP-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-
CC       Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family. {ECO:0000255|HAMAP-Rule:MF_01458}.
DR   EMBL; CP001825; ACZ41094.1; -; Genomic_DNA.
DR   RefSeq; WP_012874129.1; NC_013525.1.
DR   SMR; D1CDT8; -.
DR   STRING; 525904.Tter_0172; -.
DR   EnsemblBacteria; ACZ41094; ACZ41094; Tter_0172.
DR   KEGG; ttr:Tter_0172; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   OMA; QHESIDH; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; TTER525904:G1GGS-176-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDT8.
DR   SWISS-2DPAGE; D1CDT8.
KW   ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN         1    646       ATP-dependent zinc metalloprotease FtsH.
FT                                /FTId=PRO_0000400408.
FT   TOPO_DOM      1     35       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   TRANSMEM     36     56       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   TOPO_DOM     57    144       Extracellular. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   TRANSMEM    145    165       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   TOPO_DOM    166    646       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   NP_BIND     237    244       ATP. {ECO:0000255|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    460    460       {ECO:0000255|HAMAP-Rule:MF_01458}.
FT   METAL       459    459       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   METAL       463    463       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
FT   METAL       535    535       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01458}.
SQ   SEQUENCE   646 AA;  71765 MW;  B43BAD92DB2F51C1 CRC64;
     MTNNQTDRPR PPGPESRRFD NNDKNNRNRW GPIPSWAWIV LIVALLLNWL VAPILFPEGK
     GAVSIPYTSF KQQLENNNVA EVTTQADKIT GEFKQAVKVP GVDQPVKRFV THIPAFGDDQ
     LMSQLDQKGV IVNVQPESST RSLLLSILIS FGPTILFFLL FLWLISKAQS SQQGLFGLGK
     SRAKRYNATE STRVTFDDVA GIEEAKQELA EIVDFLKNPQ KYQRLGGTIP KGVLLIGPPG
     TGKTLLARAV AGEAGVPFFS MSGSEFVEMI VGVGAARVRE LFQQAKKEAP CIIFVDELDA
     IGRRRGSSIN VGGHDEREQT LNQLLVEMDG FDSRQGVIVL AATNRPDVLD PALLRPGRFD
     RRVVVQRPDK VGRLKILQVH TRNVPLDPNL DLSEIAAATP GLVGADLRNL VNEAALLAAR
     RGKNYVDRED FFDALEKITL GAERKLLISE EDRRRVAYHE SGHALLGLLL PEADPVHKVT
     IIPRGQALGV TYQTPEDDRY NYTERYLRSR ITAALGGRAA EELVFGTVTT GAENDLKQVT
     EIARQMVTRW GMSKEVGLVY LSPDGQEDFL GPNPITSREY SESLATVIDR ETRRIIDECY
     AEALSLLNRE RQRLDNLAEA LLREESLDEQ QIREIVGLGE KQPEPA
//

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