FTSK_VIBCH
ID FTSK_VIBCH Reviewed; 960 AA.
AC Q84I33; Q9KQU5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=VC_1903;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-917.
RX PubMed=12562793; DOI=10.1128/jb.185.4.1236-1244.2003;
RA Herz K., Vimont S., Padan E., Berche P.;
RT "Roles of NhaA, NhaB, and NhaD Na(+)/H(+) antiporters in survival of Vibrio
RT cholerae in a saline environment.";
RL J. Bacteriol. 185:1236-1244(2003).
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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {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 multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AE003852; AAF95051.1; -; Genomic_DNA.
DR EMBL; AF489522; AAO37927.1; -; Genomic_DNA.
DR PIR; A82142; A82142.
DR RefSeq; NP_231537.1; NC_002505.1.
DR RefSeq; WP_000471965.1; NZ_LT906614.1.
DR AlphaFoldDB; Q84I33; -.
DR SMR; Q84I33; -.
DR STRING; 243277.VC_1903; -.
DR DNASU; 2613532; -.
DR EnsemblBacteria; AAF95051; AAF95051; VC_1903.
DR GeneID; 57740536; -.
DR KEGG; vch:VC_1903; -.
DR PATRIC; fig|243277.26.peg.1819; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_0_2_6; -.
DR OMA; SWLTIVD; -.
DR BioCyc; VCHO:VC1903-MON; -.
DR Proteomes; UP000000584; 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-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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..960
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098316"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 601..814
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 621..626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 960 AA; 105888 MW; 0AA778438B7D8970 CRC64;
MFKENKNKVE TIIKTSEEAP SSRLNGSQRL KESGLILAFL FSIFLAVALF SFNPADPSWS
QTAWGTDIHN AGGLVGAWLA DTLFFVFGSL AYPLPFITAF AAWVLLRKRD EGDEIDFTLW
GTRLLGLTIV LLTSCGLADI NFDDIWYFSS GGVIGDVLTS LALPTLNILG TTLVLLFLWG
AGITLLTGIS WLRIVEWIGE RSIAAFVGLF NRLRGEKAER VKPALVKPEL PVEELEPTFS
ASMDTEIDEP APSLRRFNIH MPEERDVPDI HFEPQVEPKV ELKPEPPRQR EPAPHFSRVA
AQNTQVEPVS SARTQQWDAT IEELEQQARL VDDYAVEDDA VPSVLTSSTL SDVEDSILTT
AISVDEEEES LSENFNHSFN IEVEDEEVEP SIANLHWSDD EDELEETPSV MVSPAIESDW
EDEDEPDDRD VAAFQNIVSQ AQANAAAQQN PFLVQKAVNL PKPTEPMPTL ELLYHPEKRE
NFIDREALEE IARLVESKLA DYKIQAQVVD IFPGPVITRF ELDLAPGVKV SRISSLSMDL
ARSLSAMAVR VVEVIPGKPY VGLELPNMSR QTVYLSDVIA SPQFKESKSP TTVVLGQDIA
GDAVVADLSK MPHVLVAGTT GSGKSVGVNV MILSMLYKAS PEDVRFIMID PKMLELSVYE
GIPHLLAEVV TDMKDASNAL RWCVGEMERR YKLMSVLGVR NIKGFNDKLR MAAEAGHPIY
DPLWKDGDSM ESEPPLLEKL PYIVVVVDEF ADLMMVVGKK VEELIARLAQ KARAAGIHLI
LATQRPSVDV ITGLIKANIP TRVAFTVSTK TDSRTILDQS GAESLLGMGD MLYLPAGSSH
TIRVHGAFAS DDDVHAVVNN WKARGKPNYI SEIIQGDHGP EALLPGEQSE SDEELDPLFD
QVVEHVVETR RGSVSGVQRR FKIGYNRAAR IVEQLEAQGI VSAPGHNGNR DVLAPAPIRD
