ID A0A0A7I3H3_9BIFI Unreviewed; 932 AA.
AC A0A0A7I3H3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AIZ14843.1};
GN ORFNames=AH68_07095 {ECO:0000313|EMBL:AIZ14843.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ14843.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ14843.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ14843.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP007456; AIZ14843.1; -; Genomic_DNA.
DR RefSeq; WP_039199948.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I3H3; -.
DR STRING; 1447716.AH68_07095; -.
DR KEGG; bka:AH68_07095; -.
DR HOGENOM; CLU_001981_2_2_11; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000030625; Chromosome.
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:AIZ14843.1};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..760
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 577..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 932 AA; 100116 MW; 848D4B1677F75160 CRC64;
MARTASSNTK SSGKRSAGKA RSGETKVMDA AEPSPVMGVL TKYRRDITCF VLVILAVLFC
ASEWFRVQGA FGQVLHAMAS GLFGLMSVIL PVFLMLVVFS LMHKTQRKSD NARMAAGWSM
ILWSICSILD AALASDIQGF DMALLQKAGG LLGYVLGCPL AWGLSKAFAI VIFAVVILFS
LLLITRTRVD EVPDKICALM SRFGFGANKA DDDETEQFPN EVRIGDTTLS FAEGVPAHDG
TDNAAAEGKG PMLLSRLKQL ISSKTKKQGT QDGLEYYDGD EAFRNAAEQH GETAETMLDE
PYQSVSQPRS ISSGEHSTQD SGGTVVMPQM PVARSLSSDP IGTASGTMPQ ISETVPAMVG
AVPSSEIKSV GVAADDPWAV IDENGTSNGT QVMVDAATNE VVNDLNGGLS EEGFSDESDE
IPEGPYHLPD LGMLKQGAPH AVHTPENDRV IRALTVTFQQ FNVDAKVIGF LRGPSVTMYE
VELGPGVKVE KVTNLQKNIA YAVASSDVRI LSVIEGKSAI GIEIPNTDRE TVVLGDVLRS
DKARNDPNPM LTGVGKDVEG HFITADLTKM PHLLVAGATG SGKSSFINSM LTSVIMRATP
DQVRMIMVDP KRVELSAYAG IPHLLTPIIT DPKKAAQALE WVVKEMDARY SDLEFFGFRH
IKDFNAAVRA GKVHAPAGSK RKVAPYPYIL VVVDEMADLM MVAKNDVESS IQRITQLARA
AGVHLVLATQ RPSVDVVTGL IKANIPSRLA FATSSATDSR VILDSTGAET LIGQGDALFL
PMGQAKPLRV QGAWVDESEI RRAVEFVRTQ RKPHYREDIE EMAKESDKKA IEPDEDIGGD
MDVLLQAAEL VVTSQFGSTS MLQRKLRVGF AKAGRLMDLL ESRGIVGPSE GSKAREVLVQ
PQDLPQVLAF IKGETSSLNS GASSAVDSEV AM
//
