ID A0A239VKY6_9MICO Unreviewed; 901 AA.
AC A0A239VKY6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Stage III sporulation protein E {ECO:0000313|EMBL:SNV22258.1};
GN Name=spoIIIE {ECO:0000313|EMBL:SNV22258.1};
GN ORFNames=SAMEA4475696_01462 {ECO:0000313|EMBL:SNV22258.1};
OS Dermatophilus congolensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Dermatophilus.
OX NCBI_TaxID=1863 {ECO:0000313|EMBL:SNV22258.1, ECO:0000313|Proteomes:UP000242637};
RN [1] {ECO:0000313|EMBL:SNV22258.1, ECO:0000313|Proteomes:UP000242637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13039 {ECO:0000313|EMBL:SNV22258.1,
RC ECO:0000313|Proteomes:UP000242637};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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}.
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DR EMBL; LT906453; SNV22258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239VKY6; -.
DR STRING; 1121387.GCA_000429885_02128; -.
DR KEGG; dco:SAMEA4475696_1462; -.
DR Proteomes; UP000242637; Chromosome 1.
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};
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:UP000242637};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 502..702
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 901 AA; 96708 MW; 390E197C7CA6B3D0 CRC64;
MATRNTPNKR RTAAKGKPVP RKNPRTKNGA ATRRTPAAKT PRAGSGTPSR GAGSALRGIT
GLTGGMARRV GRTASGLPEE HRRDGMGLFF IIIAVIIAAR EWWGLPGPLG EFIHIIAAGT
IGWGALFLPL AFVWFGLRIM RNPVEDAATS RIAIGVTTLT VSLAGIIHIA RGNPRISGGT
EAFRSAGGMI GYLVGAPLDA MLTDWGAYVV LAIVAFFGVL VITATPFVEI PDRLTELHDR
LFGLDEYVDT IPIPTSSRRK SRRNLELDHR DGDEAFEQAA EVHKGRSRRL ADLPKIAAEE
AANAQRDTTT AADRAATQAL DRVNNPAAAS STKPGPVPAT NQTELVPPPT QAIPQRTEQL
ALAGDVTYTL PPSDLLEQGT PHKTRSEVND HVVQALTGVL EQFNINAQVT GFSRGPTVTR
YEVELGAGTK VERVTALSKN IAYAVASADV RILSPIPGKS AIGIEIPNTD REKVSLGDVL
RSQVATRNPH PMVMGVGKDV EGGFVIANLA KMPHLLVAGA TGSGKSSFVN SMITSILVRS
TPDEVRLILV DPKRVELTAY EGIPHLITPI ITNPKKAAEA LQWVVKEMDA RYDDLAAFGY
KHIDDFNKAV RSGDVKLPPG SQRVVEPYPY LLVVVDELAD LMMVAPRDVE ESIVRITQLA
RAAGIHLVLA TQRPSVDVVT GLIKANVPSR MAFATSSLAD SRVVLDQPGA EKLIGQGDAL
FLPMGASKPM RVQGAWVPES EVAAVVKFVT DQLKPSYRED VVPATEKKQI DADIGDDLEL
LLEATKQVVT TQFGSTSMLQ RKLRVGFAKA GRLMDLMESR GVVGPSEGSK ARDVLIRPED
LPTVLAQMQG QTPPPPAEGQ QGTAGGHDRY ADVEVQGEEV VHEGDLEDED AWQLTQQGRG
R
//
