ID A0A1A9T426_9PROT Unreviewed; 768 AA.
AC A0A1A9T426;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OAM52760.1};
GN ORFNames=A7981_04745 {ECO:0000313|EMBL:OAM52760.1};
OS Methylovorus sp. MM2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=1848038 {ECO:0000313|EMBL:OAM52760.1, ECO:0000313|Proteomes:UP000077545};
RN [1] {ECO:0000313|Proteomes:UP000077545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|Proteomes:UP000077545};
RA Macey M.C., Murrell J.C.;
RT "Draft genome of Methylovorus sp. MM1 isolated from grassland soil.";
RL Submitted (MAY-2016) 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. 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 -!- 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:OAM52760.1}.
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DR EMBL; LXUF01000001; OAM52760.1; -; Genomic_DNA.
DR RefSeq; WP_067264728.1; NZ_LXUF01000001.1.
DR AlphaFoldDB; A0A1A9T426; -.
DR STRING; 1848038.A7981_04745; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000077545; 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:OAM52760.1};
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:UP000077545};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 413..622
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 430..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 768 AA; 83908 MW; 1E1EB83944F7A0ED CRC64;
MFFSKNKLPL NSRREVAPPP SEGTGLIKEA WWLALVVVGI YLTVILATYQ PQDPSWSHSA
SNSDVVHNAG GTVGAWLSDI LLFLFGFSAW WWAVFAFYAI WLVYLRLEVV AASERPLLLF
NIVGFFMLLA ASCALEFGHL VHLPAELPSA SGGMLGSVLD GLLQSMLGFT GSTMILLLLM
ATGFSLFTGW SWIVMTEKLG GALESSYFFI QNKLQDRQDR KLGRVAEQLR EEFVDSERKR
TEDRPPVQIE VPVLEIAKSD RVEKERQSPL FETMPDSPLP PLHLLDEPTG AVEVQSAETL
DFTSRLIERK LMDFGIEVKV ITALPGPVIT RYELEPAAGV KGSQVANLSK DLARALSVVS
IRVVETIPGK AYMGLEIPNP KRQIVFLSEI LGSQVYADVT SPLAIAMGKD IAGKPVVADL
AKMPHVLVAG TTGSGKSVAI NAMILSLLYK AEPSKVRLIL IDPKMLELSV YEGIPHLLAP
VITDMRQAGN ALNWSVAEME RRYKLMSVLG VRNLAGYNQK IRDAEKEGTS IPHPFTLTPE
SPEPLEELPL IVVVIDELAD LMMVVGKKVE EPIARLAQKA RACGIHLVVA TQRPSVDVIT
GLIKANIPTR VAFQVSSKID SRTILDQMGA EALLGQGDML YQPPGTSYPQ RIHGAFVSDQ
EVHRVVEHIK SLGEPNYIEG ILTGGVDENA EGGLSGESGS GSEADPLYDE AVAIVLKSRR
ASISAVQRNL RIGYNRAARL IEEMERAGLV SAMQSNGNRE VLAPNNQE
//
