ID E2SEG9_9ACTN Unreviewed; 767 AA.
AC E2SEG9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:EFQ82446.1};
GN ORFNames=HMPREF0063_12428 {ECO:0000313|EMBL:EFQ82446.1};
OS Aeromicrobium marinum DSM 15272.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ82446.1, ECO:0000313|Proteomes:UP000003111};
RN [1] {ECO:0000313|EMBL:EFQ82446.1, ECO:0000313|Proteomes:UP000003111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ82446.1,
RC ECO:0000313|Proteomes:UP000003111};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) 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 -!- 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:EFQ82446.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACLF03000007; EFQ82446.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SEG9; -.
DR STRING; 585531.HMPREF0063_12428; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_2_2_11; -.
DR Proteomes; UP000003111; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000003111};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 416..616
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 201..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 767 AA; 81846 MW; AFED1A1DB86F9184 CRC64;
MARAVTGLGR LLRAIWLGLA GVIGAIARSI GRSARDLDPA HRRDGVGLAV LGLGMVVAAA
TWWQLPGAAG RVIRQVCEGT VGVLSVGVPV VLAIIAWRTL RHPDEQGPAG RQVIAWLAVG
GGVLGLVHLS NGVPRPGDMA AVREAGGALG YLFSAVPMDL LKTGYVVAPL LVLVVAFGVL
VLSNTPVHAV PERLRATRDR ILGRPQEAEP APSARRSHPR TPAAPVVDEP YENPLIDVPD
DVTDDPAPAV HETAPVEEAQ LPPLEPLPAR AEQLALSGDV IYSLPDSTVL REGSPHKARS
AASDEVVERL TEVLEQFQID AQVTGYTRGP TVTRYEVELG PAVKVEKVTA LSKNIAYAVA
SNEVRILSPI PGKSAIGVEI PNVDKEMVSL GDVLRSTKAR SDHHPMVIGL GKDVEGGFVV
ANLAKMPHLL VAGATGSGKS SFVNSMISSI LMRSTPDEVR MIMVDPKRVE LTAYEGIPHL
ITPIITNPKK AAEALQWVVR EMDMRYDDLA NFGFRHIDDF NAAVRAGTVE LPALSERVLA
PYPYLLVVVD ELADLMMVAP RDVEDSVVRI TQLARAAGIH LVLATQRPSV DVVTGLIKAN
VPSRLAFATS SLADSRVILD QPGAEKLVGQ GDGLFLPMGV NKAMRMQGAW ITEAEIHAVV
EHCKTQLQPS YRDDVTAPAQ SKRELDDDIG DDLDLVLQAV ELVVTTQFGS TSMLQRKLRV
GFAKAGRLMD IMESRGVVGP SEGSKARDVL IKPDELEQVL ATIGAGA
//
