(data stored in ACNUC7421 zone)

HOGENOM: ECOL6_1_PE1001

ID   ECOL6_1_PE1001                       STANDARD;      PRT;   1347 AA.
AC   ECOL6_1_PE1001; Q8FJC7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA translocase ftsK; (ECOL6_1.PE1001).
GN   Name=ftsK; OrderedLocusNames=c1027;
OS   ESCHERICHIA COLI O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOL6_1.PE1001.
CC       Escherichia coli O6 (strain UPEC / O6:H1 / ATCC 700928 / CFT073)
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:FTSK_ECOL6
CC   -!- FUNCTION: DNA motor protein, which is both required to move DNA
CC       out of the region of the septum during cell division and for the
CC       septum formation. Tracks DNA in an ATP-dependent manner by
CC       generating positive supercoils in front of it and negative
CC       supercoils behind it. Also plays a role in resolution of dimer
CC       chromosomes by regulating the xerC and xerD recombination complex,
CC       possibly by switching the catalytic state of the two recombinases.
CC       Required for the targeting of ftsQ, ftsL and ftsI to the septum
CC       (By similarity).
CC   -!- SUBUNIT: Homohexamer. This suggests the formation of a ring
CC       between the two cells at the septum that surrounds DNA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein; Cytoplasmic side. Note=Located at the septum. The large
CC       C-terminal part of the protein is cytoplasmic (Potential).
CC   -!- SIMILARITY: Contains 1 FtsK domain.
CC   -!- GENE_FAMILY: HOG000010001 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8FJC7; -.
DR   EMBL; AE014075; AAN79499.1; -; Genomic_DNA.
DR   RefSeq; NP_752956.1; NC_004431.1.
DR   ProteinModelPortal; Q8FJC7; -.
DR   SMR; Q8FJC7; 858-1266, 1279-1347.
DR   EnsemblBacteria; EBESCT00000041945; EBESCP00000040294; EBESCG00000040995.
DR   GeneID; 1038631; -.
DR   GenomeReviews; AE014075_GR; c1027.
DR   KEGG; ecc:c1027; -.
DR   NMPDR; fig|199310.1.peg.999; -.
DR   GeneTree; EBGT00050000008749; -.
DR   OMA; YQPEPAP; -.
DR   ProtClustDB; PRK10263; -.
DR   GO; GO:0016021; C:integral to 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   InterPro; IPR002543; Cell_div_FtsK/SpoIIIE.
DR   InterPro; IPR018541; DNA_translocase_Ftsk_gamma.
DR   Pfam; PF09397; Ftsk_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00843; Ftsk_gamma; 1.
DR   PROSITE; PS50901; FTSK; 1.
DR   HOGENOMDNA; ECOL6_1.PE1001; -.
KW   AAN79499.1000068575old_1320000031;
KW   DNA translocase ftsK ;
KW   ATP-binding; Cell cycle; Cell division; Cell inner membrane;
KW   Cell membrane; Chromosome partition; Complete proteome; DNA-binding;
KW   Membrane; Nucleotide-binding; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1347 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQEYTEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
     HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL
     ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
     WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
     RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDEEEITY TARGVAADPD DVLFSGNRAT
     QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPTQPTVAW
     QPVPGPQTGE PVIAPAPEGY PHQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPVQQPY
     YAPAAEQPVQ QPYYAPAPEQ PVAGNAWQAE EQQSTFAPQS TYQTEQTYQQ PAAQEPLYQQ
     PQPVEQQPVV EPEPVVEETK PTRPPLYYFE EVEEKRARER EQLAAWYQPI PEPVKEPEPI
     KSSLKAPSVA AVPPVEAAAA VSPLASGVKK ATLATGAAAT VAAPVFSLAN SGGPRPQVKE
     GIGPQLPRPK RIRVPTRREL ASYGIKLPSQ RAAEEKAREA QRNQYDSGDQ YNDDEIDAMQ
     QDELARQFAQ TQQQRYGEQY QHDVPVNTED ADAAAEAELA RQFAQTQQQR YSGEQPAGAN
     PFSLDDFEFS PMKALLDDGP HEPLFTPIVE PVQQPQQPVA PQQQYQQPQQ PVAPQPQYQQ
     PQQPVAPQPQ YQQPQYQQPQ QPVAPQQQYQ QPQQPVTQQP QYQQPQQPVV PQPQDTLLHP
     LLMRNGDSRP LHKPTTPLPS LDLLTPPPSE VEPVDTFALE QMARLVEARL ADFRIKADVV
     NYSPGPVITR FELNLAPGVK AARISNLSRD LARSLSTVAV RVVEVIPGKP YVGLELPNKK
     RQTVYLREVL DNAKFRDNPS PLTVVLGKDI AGEPVVADLA KMPHLLVAGT TGSGKSVGVN
     AMILSMLYKA QPEDVRFIMI DPKMLELSVY EGIPHLLTEV VTDMKDAANA LRWCVNEMER
     RYKLMSALGV RNLAGYNEKI AEADRMMRPI PDPYWKPGDS MDAQHPVLKK EPYIVVLVDE
     FADLMMTVGK KVEELIARLA QKARAAGIHL VLATQRPSVD VITGLIKANI PTRIAFTVSS
     KIDSRTILDQ AGAESLLGMG DMLYSGPNST LPVRVHGAFV RDQEVHAVVQ DWKARGRPQY
     VDGITSDSES EGGVGGFDGA EELDPLFDQA VQFVTEKRKA SISGVQRQFR IGYNRAARII
     EQMEAQGIVS EQGHNGNREV LAPPPFD
//

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