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Database: UniProt
Entry: A0A158K140_9BURK
LinkDB: A0A158K140_9BURK
Original site: A0A158K140_9BURK 
ID   A0A158K140_9BURK        Unreviewed;      1172 AA.
AC   A0A158K140;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:SAL74190.1};
GN   ORFNames=AWB68_04549 {ECO:0000313|EMBL:SAL74190.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL74190.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; FCON02000055; SAL74190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158K140; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
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   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; 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}; Cell cycle {ECO:0000313|EMBL:SAL74190.1};
KW   Cell division {ECO:0000313|EMBL:SAL74190.1};
KW   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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          817..1026
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          132..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         834..841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1172 AA;  122315 MW;  B29E897228D349A6 CRC64;
     MHTVVLGWFG GSVVWFVPLL WRLAKSMLPG GDGLRGPGTI RLWLGFVGVL VASMALEGAL
     LGSFEAAAGV NRCGHALANA LAGLAGRVGG GSIAAAALLV CLPWLCDFQW RSAIGWANVA
     FGLGFNPQWF DAREKTPREK PSRKRRARGE PAHRAGGIPG RIAHDAPMLG MPAATSREGG
     RYQRPTVWRP PAIQRGDVKR STAAASPSVD VFADRNANAP RNPAPATGRA IPRDLVEPVA
     PIGWLGSGSG MRAGSREGAG SSKVANPGTV RPVTAPAASR GFVRTDAPAA APSAAPRTTV
     AASAVHAVQP SRSSVKRPAA SMSRPATGSV AAPSAATSRA PVHSRPAEPP GPLPAPDSIQ
     ATLRSIEENA ARWTTLAGAG LASGREPQER QPGLQGGSDH SGATRAAGET PKSANAPPIG
     DAVRSNAISA AGSSAPSFAL HAITGDVASG AGNAPTEARV APPPVDSERR RDDEAAPEDA
     LKSAPAATAL RETEAMPQRV PGQNTPLVSD TTATSLASAT PEGSARSDGT LTGETTGVEA
     LQAAAASGAA LTGTAWAMTT PRPAAALEPT QPLSPPAQSP SDTLPWLAAV VRPEAHRPAP
     PLPLQIGNTE AENDDTNPAA HQPASNVVRF PGVAIAPTAS PIGEQSAEEP PEATQPGTPR
     APIRGFTPTE FEFHAPAASA VELPGFDLLE RASDDIEPVS EERLAETGQL IEQRLQEFKV
     PVTVVGASAG PVITRFEVEP ALGVRGSQIV GLMKDLSRGL GLTSIRVVET IPGKTCMGLE
     LPNAKRQMIR LSEILEDDVY RNSKSNLTIA MGKDIVGNPV VTDLARAPHM LVAGTTGSGK
     SVAVNAMILS LLYKAKPEDV RLIMIDPKML ELSVYEGIPH LLAPVVTDMK LAANALNWCV
     GEMEKRYRLM SAVGVRNLQG FNQKVRNADA AGRKLTNPFS LTPDAPEPLS TLPMIVVIID
     ELADLMMVAG KQIEQLIARL AQKARAAGIH LILATQRPSV DVITGLIKAN IPTRVAFQVS
     SKIDSRTILD QMGAESLLGA GDMLFLPPGT GYPQRVHGAF VADDEVHRVV EYLKQFGEPE
     YEEGILSGPA SEGAAQDLFG EAPDAEADPL YDEAVSFVVR TRRASISSVQ RQLRIGYNRA
     ARLVEQMETA GLVSPMGNNG NREVLAPPGP AE
//
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