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FTSK_STRA5
ID   FTSK_STRA5              Reviewed;         816 AA.
AC   Q8CX05;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=SAG1529;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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 difSL
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the XerS 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}.
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DR   EMBL; AE009948; AAN00396.1; -; Genomic_DNA.
DR   RefSeq; NP_688523.1; NC_004116.1.
DR   RefSeq; WP_000231579.1; NC_004116.1.
DR   AlphaFoldDB; Q8CX05; -.
DR   SMR; Q8CX05; -.
DR   STRING; 208435.SAG1529; -.
DR   EnsemblBacteria; AAN00396; AAN00396; SAG1529.
DR   KEGG; sag:SAG1529; -.
DR   PATRIC; fig|208435.3.peg.1538; -.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   OMA; MTKEPEI; -.
DR   Proteomes; UP000000821; 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; IPR003593; AAA+_ATPase.
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; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00382; AAA; 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..816
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098302"
FT   TRANSMEM        35..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..816
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          475..671
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         495..500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   816 AA;  90712 MW;  FD3AEC777CBC59B4 CRC64;
     MVFMANKKKT KGKKTRRPTK AEIERQRAIQ RMITALVLTI ILFFGIIRLG IFGITVYNVI
     RFMVGSLAYL FIAATLIYLY FFKWLRKKDS LVAGFLIASL GLLIEWHAYL FSMPILKDKE
     ILRSTARLIV SDLMQFKITV FAGGGMLGAL IYKPIAFLFS NIGAYMIGVL FIILGLFLMS
     SLEVYDIVEF IRAFKNKVAE KHEQNKKERF AKREMKKAIA EQERIERQKA EEEAYLASVN
     VDPETGEILE DQAEDNLDDA LPPEVSETST PVFEPEILAY ETSPQNDPLP VEPTIYLEDY
     DSPIPNMREN DEEMVYDLDD DVDDSDIENV DFTPKTTLVY KLPTIDLFAP DKPKNQSKEK
     DLVRKNIRVL EETFRSFGID VKVERAEIGP SVTKYEIKPA VGVRVNRISN LSDDLALALA
     AKDVRIETPI PGKSLIGIEV PNSEIATVSF RELWEQSDAN PENLLEVPLG KAVNGNARSF
     NLARMPHLLV AGSTGSGKSV AVNGIISSIL MKARPDQVKF MMIDPKMVEL SVYNDIPHLL
     IPVVTNPRKA SKALQKVVDE MENRYELFSK IGVRNIAGYN TKVEEFNASS EQKQIPLPLI
     VVIVDELADL MMVASKEVED AIIRLGQKAR AAGIHMILAT QRPSVDVISG LIKANVPSRI
     AFAVSSGTDS RTILDENGAE KLLGRGDMLF KPIDENHPVR LQGSFISDDD VERIVGFIKD
     QAEADYDDAF DPGEVSETDN GSGGGGGVPE SDPLFEEAKG LVLETQKASA SMIQRRLSVG
     FNRATRLMEE LEAAGVIGPA EGTKPRKVLM TPTPSE
 
 
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