ID A0A0J0YRL1_9NEIS Unreviewed; 1069 AA.
AC A0A0J0YRL1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KLT72769.1};
GN ORFNames=PL75_06750 {ECO:0000313|EMBL:KLT72769.1};
OS Neisseria arctica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT72769.1, ECO:0000313|Proteomes:UP000036027};
RN [1] {ECO:0000313|EMBL:KLT72769.1, ECO:0000313|Proteomes:UP000036027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT72769.1,
RC ECO:0000313|Proteomes:UP000036027};
RA Hansen C.M., Hueffer K., Choi S.C.;
RT "Genome of a novel goose pathogen.";
RL Submitted (NOV-2014) 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 -!- 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:KLT72769.1}.
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DR EMBL; JTDO01000009; KLT72769.1; -; Genomic_DNA.
DR RefSeq; WP_047761155.1; NZ_JTDO01000009.1.
DR AlphaFoldDB; A0A0J0YRL1; -.
DR STRING; 1470200.PL75_06750; -.
DR PATRIC; fig|1470200.3.peg.2573; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000036027; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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; 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; 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:0000313|EMBL:KLT72769.1};
KW Cell division {ECO:0000313|EMBL:KLT72769.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000036027}.
FT DOMAIN 710..919
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 41..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..90
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 727..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1069 AA; 117092 MW; 07D2D3E5E5787B2B CRC64;
MLWIFLLIIL VGAIACVLWV RHRQEQEWMR ELTYLSRHEN GEKNSGAAEM KPAKEIRGAD
PNLQNIRQSH KAAEEARQVY EKTVAKLREL SPKHSRKLDA ISGRNMPSEN DNLDDLPIFA
ALPKTEEFAE VDDNNSVPKP VNPEQSEAAE ASVHQLKAEP LEAAREDNGN DRAHDIPMFG
AVLEPMVKPA EAVRSGKAMA PAPYLTFEES EYRPVKKVDA DLPVITLEEA TRSLHETPLA
DLIKSPEEET VATVKTPPPA DLEVVDINWH FKPALEMEGI QTPKPPVELK TISPDDPALV
RTRNRTLAEV QKISHDVPKT EARPAAIGDA SAAPKIIGED DIRSNLLRQR LARRRQVSAE
SPVQEVIPNV IPEGEILANL AKTDSPVNRQ RIRRVSTAMR ESVIPEAARV EQSHAIRLQT
PKATAPISTR FTPYTAAVIP APTATVVEPP PVPEIEMPAI DIPPPPVFQE AEIYPHVADE
VEILPEPAPV TASAHISDTP RWSITDRLIS ESAAVFTEHV PQRSPLAEVL GEETFEPEAE
EGQCGTSPAP MQQAQTQTQT QTANPAVHMP SENRLPSVDL LLPPQYDPSA AQTEEALLEN
SITIEEKLAE FKVKVKVMDA YAGPVITRYE IEPDVGVRGN AVLNLEKDLA RSLSVASIRV
VETIPGKSCM GLELPNPKRQ MIRLSEIFNA PAFQDSKSKL TLALGQDITG EPVVTDLAKA
PHLLVAGTTG SGKSVGVNAM ILSMLFKATP EEVRMIMIDP KMLELSIYEG IPHLLAPVVT
DMKLAANALN WCVNEMEKRY RLMSHMGVRN LAGFNQKVAE AAARGEKLAN PFSLTPADPE
PLEKLPFIVV VVDEFADLMM TAGKKIEELI ARLAQKARAA GIHLILATQR PSVDVITGLI
KANIPTRIAF QVSSKVDSRT ILDQMGAENL LGQGDMLFLP PGTGYPQRVH GAFASDEEVH
KVVEYLKQFG EPNYVDDILT AGVGSDDMFS NANSGRNNDG ELDPMYDEAV ACVLKTRKAS
ISSVQRQLRI GYNRAARLID QMEADGIVSA PETNGNRTVL APPNNESLD
//
