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Database: UniProt
Entry: J2U726_9BURK
LinkDB: J2U726_9BURK
Original site: J2U726_9BURK 
ID   J2U726_9BURK            Unreviewed;       931 AA.
AC   J2U726;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=DNA segregation ATPase, FtsK/SpoIIIE family {ECO:0000313|EMBL:EJL86982.1};
GN   ORFNames=PMI16_03021 {ECO:0000313|EMBL:EJL86982.1};
OS   Herbaspirillum sp. CF444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL86982.1, ECO:0000313|Proteomes:UP000007296};
RN   [1] {ECO:0000313|EMBL:EJL86982.1, ECO:0000313|Proteomes:UP000007296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF444 {ECO:0000313|EMBL:EJL86982.1,
RC   ECO:0000313|Proteomes:UP000007296};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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.
CC       {ECO:0000256|ARBA:ARBA00024784}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJL86982.1}.
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DR   EMBL; AKJW01000065; EJL86982.1; -; Genomic_DNA.
DR   RefSeq; WP_007880904.1; NZ_AKJW01000065.1.
DR   AlphaFoldDB; J2U726; -.
DR   STRING; 1144319.PMI16_03021; -.
DR   PATRIC; fig|1144319.3.peg.3062; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000007296; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          577..786
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          115..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         594..601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   931 AA;  99696 MW;  E40F538D4B6673A0 CRC64;
     MRLFLLDWFG WSFLWILPLL GRVVVSLLSG KGLRGRGSIR IWLGTLMVLC ASSAVEAMLR
     SQGDIALDSD FFGQALARGI TAGVGKLIGV LALMASGLLG LFWLFGRSRK AVAGDEPDTA
     GLPVQASVPR RTQANIPPTV RNLPASQAPK LVKAQTPPQP LQPFGNLTRN LPHKRDPWPL
     PNEMPRSANP SQTPAGNWPT APRSTEQPLK RPARPASEWA PFEALRPTQA MLARSTSTQA
     AEPAPAHQAA PKPTLATSII SKPRITPIPG SSTKVRISTA SDRSQAIPTS LSATLAARLP
     SHAATPALPQ VAQAAPAVTP GFTPAVPTSA GMQQIPAETI PTPLPFDLPE PEAVIAPEPF
     SIIDTRVEPV WESVAAPTAP AAPAPLAAET PLLFDVPEQP YTAAPAAPMQ IRTWTQAPVA
     APQPATSATV ETFTPYRPTD IPLPGIDLLD QGSDMPVEMD EAQLVEIGQL IEQRLKEFKV
     PVTVLGAYAG PVITRFEIEP ALGVRGAQIV NLMKDLARAL GLTSIRVVET IPGKTCMGLE
     LPNPKRQMIR LAEIIQSEAY ARSASHLTMA MGKDITGVPV ATDLARAPHM LVAGTTGSGK
     SVAINAMILS LLYKATPDDV RLIMIDPKML ELSVYDGIPH LLAPVVTDMK LAAHALSWCV
     AEMDKRYRLM SALGVRNLAG YNQKIADGIA AEKYVRNPFS LTPDAPEPLD RLPMIVVVID
     ELADLMMVAG KKIEELIARL AQKARAAGIH LILATQRPSV DVITGLIKAN IPTRVAFQVS
     SKIDSRTVLD QMGAETLLGH GDMLFLPPGS GYPQRVHGAF VSDEEVHRVV EHLKAHGEPQ
     YEEAILAGPA SEEPQQGDMF GEPGDESDPL YDEAVAYVTR SRRASISSVQ RQFRIGYNRA
     ARLVEQMEAA GILSSMSKSG SRDVLAPPPP D
//
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