ID A0A258NTZ0_9BURK Unreviewed; 781 AA.
AC A0A258NTZ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OYY33785.1};
GN ORFNames=B7Y60_17900 {ECO:0000313|EMBL:OYY33785.1};
OS Polaromonas sp. 35-63-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY33785.1, ECO:0000313|Proteomes:UP000216365};
RN [1] {ECO:0000313|EMBL:OYY33785.1, ECO:0000313|Proteomes:UP000216365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35-63-35 {ECO:0000313|EMBL:OYY33785.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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. 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 -!- 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:OYY33785.1}.
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DR EMBL; NCFQ01000015; OYY33785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258NTZ0; -.
DR Proteomes; UP000216365; 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: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; 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; 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:OYY33785.1};
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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 425..634
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 442..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 781 AA; 84890 MW; A7F913A445915EA8 CRC64;
MTYSLDTLNS RTSSATGPAG GVKRFAHEVS LILGLLALVF WLGALISYSP LDAAWSTTGS
SEAASALKAG EAVTRNWGGR LGAHLADASY FLFGFSVWWA LAAGVRAWLG SLARGLRSQP
ASSTALDRVR FWACLALLLL ASTALEWSRL YRFEVRLPGH AGGILGYLAG PASVKWLGFT
GSGLVWIAVG VIAVSVVFAF SWAHTAQRIG AWIDELIESR REKREIAEDL AVGRVAARER
EEILHEERIE IEEHHPVPVL IEPTLVEIPK SERVAKERQK PLFSEMPDSK LPQVDLLDGA
LIRQETVAPE TLEMTSRLIE KKLKDFGVEV RVVAAAPGPV ITRYEIEPAT GVKGAQIVNL
AKDLARALSL VSIRVIETIP GKNYMALELP NAKRQSIKLS EILGSQVYNE AKSMLTIGLG
KDISGAPVVA DLAKMPHCLV AGTTGSGKSV GINAMILSLL YKADARDVRL LLIDPKMLEM
SVYEGIPHLL APVVTDMRQA AHGLNWCVAE MEKRYKLMSK MGVRNLAGYN VKIDEAKARG
EFIYNPFSLT PEQPEPLERL PYIVVVIDEL ADLMMVVGKK IEELIARLAQ KARAAGIHLV
LATQRPSVDV ITGLIKANIP TRLSFQVSSK IDSRTILDQM GAEALLGMGD MLYMPSGTGF
PVRVHGAFVS DDEVHRVVAY LKQQGEPNYI DGVLEGGTVD GEGDMLGDGN GGSEGDKDPM
YDQAVEIVLK NRKASISLVQ RHLKIGYNRA ARMLEEMEKA GMISAMSGSG QREILVPARA
E
//
