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FTSK_MYCLE
ID   FTSK_MYCLE              Reviewed;         840 AA.
AC   O05560;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=ML0977; ORFNames=MLCB33.09c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Essential cell division protein that coordinates cell
CC       division and chromosome segregation. The N-terminus is involved in
CC       assembly of the cell-division machinery. The C-terminus functions as a
CC       DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the Xer recombinase, allowing
CC       activation of chromosome unlinking by recombination (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Located at the septum. {ECO:0000250}.
CC   -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC       localization to the septal ring and is required for cell division,
CC       followed by a linker domain, and a C-terminal domain, which forms the
CC       translocation motor involved in chromosome segregation. The C-terminal
CC       domain can be further subdivided into alpha, beta and gamma subdomains.
CC       The alpha and beta subdomains form the DNA pump, and the gamma
CC       subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB08120.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC31358.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z94723; CAB08120.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583920; CAC31358.1; ALT_INIT; Genomic_DNA.
DR   PIR; C87031; C87031.
DR   RefSeq; WP_010908050.1; NC_002677.1.
DR   AlphaFoldDB; O05560; -.
DR   SMR; O05560; -.
DR   STRING; 272631.ML0977; -.
DR   EnsemblBacteria; CAC31358; CAC31358; CAC31358.
DR   KEGG; mle:ML0977; -.
DR   Leproma; ML0977; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_2_1_11; -.
DR   Proteomes; UP000000806; 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-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025199; FtsK_4TM.
DR   InterPro; IPR041027; FtsK_alpha.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR018541; Ftsk_gamma.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF13491; FtsK_4TM; 1.
DR   Pfam; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00843; Ftsk_gamma; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell membrane;
KW   Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..840
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098270"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..840
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          479..679
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         499..504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   840 AA;  89716 MW;  48F70EB38315A3A9 CRC64;
     MASKTVARSG NRTSSLKATS RGVSQSRRPV PPRPRRNRPA ERRNQSLLLA AGLTCGQAIR
     ATWLVAAKGA GGAARSIGRA RDIEPGHRRD GIALALLGLA VVVAASSWFD AARPIGAWVD
     AVLRTFIGSA VVVLPLVIAA VAVVLMRTQP NLDTRPRLIL GATLIALSFL GLRHLWSGSP
     ETPEVRRGAA GFLGFAIGGP LSDGLTAWIA APLLFIGALF GLLLLTGTTV REVPEVLRGM
     FDTGLFQRDY DDQYDAEYRY DDIPGAPPED FSGCYDGSLV GGGDAEQKVR GWPVTDLAEV
     SLQDDVPTTP EPAVQAGTAE VHRLTPRSAE EHRTQALDRA IEGSYTLPSM SLLLTGDPPK
     KCSAANNHMA SAIGGVLTQF KVDAAVTGCT RGPTVTRYEV ELGPGVKVEK ITALQKNIAY
     AVATESVRML APIPGKSAVG IEVPNTDREA VRLADVLTAP STRRDHHSLV IGLGKDIEGN
     FISANLAKMP HLLVAGSTGS GKSSFVNSML VSLLTRSTPE EVRMILIDPK MVELTPYEGI
     PHLITPIITQ PKKAAAALVW LVEEMEQRYQ DMQASRVRHI DVFNEKVRSG EITAPLGSQR
     VYRPYPYILA IVDELADLMM TAPRDVEDAI VRITQKARAA GIHLVLATQR PSVDVVTGLI
     KTNVPSRLAF ATSSLTDSRV ILDQAGAEKL IGMGDGLFLP MGASKPVRLQ GAFITDEEIH
     AVVTACKDQA EPEYTEGVTT AKTTGERTDV DPDIGDDMDV FLQAVELVVS SQFGSTSMLQ
     RKLRVGFAKA GRLMDLMETR SIVGPSEGSK AREVLVKADE LAATLALIRG GASADGSNED
 
 
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