FTSK_SALTY
ID FTSK_SALTY Reviewed; 1351 AA.
AC Q8ZQD5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=STM0960;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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. 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; AE006468; AAL19895.1; -; Genomic_DNA.
DR RefSeq; NP_459936.1; NC_003197.2.
DR RefSeq; WP_001542260.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQD5; -.
DR SMR; Q8ZQD5; -.
DR STRING; 99287.STM0960; -.
DR PaxDb; Q8ZQD5; -.
DR EnsemblBacteria; AAL19895; AAL19895; STM0960.
DR GeneID; 1252479; -.
DR KEGG; stm:STM0960; -.
DR PATRIC; fig|99287.12.peg.1012; -.
DR HOGENOM; CLU_001981_0_1_6; -.
DR PhylomeDB; Q8ZQD5; -.
DR BioCyc; SENT99287:STM0960-MON; -.
DR Proteomes; UP000001014; 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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1351
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098289"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 45..74
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 99..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 116..132
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 133..162
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 163..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 180..1351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT DOMAIN 996..1209
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 357..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1016..1021
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1351 AA; 148302 MW; 7A44DD0F0953DB5E CRC64;
MSQEYTEDKD VTLTKLSSGR RLLEALLILI ALFAVWLMAA LLSFNPSDPS WSQTAWHEPI
HNLGGAPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSTDDYIDYF AVSLRLIGVL
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIMLLCI WAAGLTLFTG
WSWVSIAEKL GGWLLNILTF ASNRTRRDDT WVDDEEYDDE YDEETDGVQR ESRRARILRG
ALARRKRLAE KFSNPRGRQT DAALFSGKRM DDDEDIQYSA RGVAADPDDV LFSGNRATQP
EYDEYDPLLN GHSVTEPVAA AAAATAVTQT WAASADPIMQ TPPMPGAEPV VAQPTVEWQP
VPGPQTGEPV IAPAPEGYQP HPQYAQPQEA QSAPWQQPVP VASAPQYAAT PATAAEYDSL
APQETQPQWQ PEPTHQPTPV YQPEPIAAEP SHMPPPVIEQ PVATEPEPDT EETRPARPPL
YYFEEVEEKR AREREQLAAW YQPIPEPVKE NVPVKPTVSV APSIPPVEAV AAAASLDAGI
KSGALAAGAA AAAPAFSLAT GGAPRPQVKE GIGPQLPRPN RVRVPTRREL ASYGIKLPSQ
RIAEEKAREA ERNQYETGAQ LTDEEIDAMH QDELARQFAQ SQQHRYGETY QHDTQQAEDD
DTAAEAELAR QFAASQQQRY SGEQPAGAQP FSLDDLDFSP MKVLVDEGPH EPLFTPGVMP
ESTPVQQPVA PQPQPQYQQP QQPVAPQPQY QQPQQPVAPQ PQYQQPQQPV APQPQYQQPQ
QPVAPQPQYQ QPQQPVAPQP QYQQPQQPVA PQPQYQQPQQ PVAPQPQYQQ PQQPTAPQDS
LIHPLLMRNG DSRPLQRPTT PLPSLDLLTP PPSEVEPVDT FALEQMARLV EARLADFRIK
ADVVNYSPGP VITRFELNLA PGVKAARISN LSRDLARSLS TVAVRVVEVI PGKPYVGLEL
PNKKRQTVYL REVLDNAKFR ENPSPLTVVL GKDIAGDPVV ADLAKMPHLL VAGTTGSGKS
VGVNAMILSM LYKAQPEDVR FIMIDPKMLE LSVYEGIPHL LTEVVTDMKD AANALRWSVN
EMERRYKLMS ALGVRNLAGY NEKIAEAARM GRPIPDPYWK PGDSMDVQHP VLEKLPYIVV
LVDEFADLMM TVGKKVEELI ARLAQKARAA GIHLVLATQR PSVDVITGLI KANIPTRIAF
TVSSKIDSRT ILDQGGAESL LGMGDMLYSG PNSTMPVRVH GAFVRDQEVH AVVQDWKARG
RPQYVDGITS DSESEGGGGG FDGGEELDAL FDQAVNFVTQ KRKASISGVQ RQFRIGYNRA
ARIIEQMEAQ GIVSAQGHNG NREVLAPPPF E
