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Database: UniProt
Entry: A0A2V5JJL6_9MICC
LinkDB: A0A2V5JJL6_9MICC
Original site: A0A2V5JJL6_9MICC 
ID   A0A2V5JJL6_9MICC        Unreviewed;       971 AA.
AC   A0A2V5JJL6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PYI37446.1};
GN   ORFNames=CVS30_15605 {ECO:0000313|EMBL:PYI37446.1};
OS   Arthrobacter psychrolactophilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=92442 {ECO:0000313|EMBL:PYI37446.1, ECO:0000313|Proteomes:UP000247980};
RN   [1] {ECO:0000313|EMBL:PYI37446.1, ECO:0000313|Proteomes:UP000247980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:PYI37446.1,
RC   ECO:0000313|Proteomes:UP000247980};
RA   Liu Q., Xin Y.-H.;
RT   "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT   and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT   glacialis sp. nov.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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. Required for activation of the Xer recombinase, allowing
CC       activation of chromosome unlinking by recombination.
CC       {ECO:0000256|ARBA:ARBA00024986}.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PYI37446.1}.
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DR   EMBL; QJVC01000022; PYI37446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5JJL6; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000247980; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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; 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   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:PYI37446.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000247980};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        87..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          548..748
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         565..572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   971 AA;  102504 MW;  01B1F1BB147C3810 CRC64;
     MATRSTSARS STGQKGSTSS RAPKTTKTPV SRSKPSASGQ EVHLVWPVRV AVSFWQGFGH
     LVGAAIRRMG TDKGAMPAEE RRDGAGLLFF LLALVTATFE WWGLTGPLAD SVRGIFQGSF
     GWFSVLLPPM FLIFSVLVFR QPSNMSTNNR VALGFSILTL AGCALAHVAA GNPNISDGFA
     GISAAGGMVG VLSGGLVANL GSVTSLIVFS LVAFASVLVL SNTPVRHIPA RLRGIYEKLM
     GTEPGYSDGA LPNGHDQSYL YEHAAESKKP RSLRARQKAA REAEDEFEDV VGTEAFATPI
     IELDDDGAPI PASKSPSLRP GVRRPTRDQL AADKIKARQG LPTSSDVFDV AADGEPVTEA
     IGVIASPTGR ATAGAGVYDF DAAATQAMPA PPLAPPTPIP ARSEQLLLSG DVTYTLPDSE
     FLPAGPPGKD ATEANDTVVA ALTDTMQQFN VDAKVTGFSR GPTVTRYEIE LAPGTKVERV
     TALSKNISYA VASSDVRILS PIPGKSAIGI EIPNADKEIV VLGDVLRSAN ARRTEHPMVM
     GVGKDVEGGF VVANLAKMPH LLVAGATGAG KSSFVNSMIV SILMRATPDE VRMVMVDPKR
     VELTAYEGVP HLITPIITNP KKAAEALQWV VREMDQRYDD LANYGFKHID EFNKAVKAGN
     VHPPVDSKRV VRPYPYLLVI VDELADLMMV APRDVEDSIV RITQLARAAG IHLVLATQRP
     SVDVVTGLIK ANVPSRMAFA TSSVTDSRVV LDQPGAEKLL GQGDALFLPM GKSKPVRVQG
     AWVTEAEIKA VVDHVKGQLK ATYREDVAAE APKKVIEDDI GDDMDVLLQA TELVVTTQFG
     STSMLQRKLR VGFAKAGRLM DLLESRGVVG PSEGSKARDV LVKPDDLAET LAAIRGDGGA
     GGGSAVGPSA GLPAAPTVDP KIAALSENAN ANHGWGGDLV ADDLASRPQA VDYNDGADDE
     DGEDAWSLTG R
//
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