ID G7Z7X6_AZOL4 Unreviewed; 645 AA.
AC G7Z7X6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK1 {ECO:0000313|EMBL:CBS85571.1};
GN OrderedLocusNames=AZOLI_0155 {ECO:0000313|EMBL:CBS85571.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85571.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FQ311868; CBS85571.1; -; Genomic_DNA.
DR RefSeq; WP_014246638.1; NC_016622.1.
DR AlphaFoldDB; G7Z7X6; -.
DR STRING; 862719.AZOLI_0155; -.
DR KEGG; ali:AZOLI_0155; -.
DR HOGENOM; CLU_001981_9_10_5; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000005667; Chromosome.
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 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 279..495
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 95..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 645 AA; 69413 MW; 630EBB4416CC9DAB CRC64;
MTPRMPHLAA PPTQAGVVTA DEFNLWCALN GRPFNLVPNP RPDGRVMWDV EVLPGTPRAG
TVYSTNLSDE ALAVVAGFAF LSGVEWAYEA RDPAEADSPA ASPAAPPCEA APAPDAASPR
APAPAAPQAA PTATGPVDYP AVYSLPTVSL LQTPPPRPVQ QHDESVLARN ARMLETVLKN
FRVRGEIMDV RPGPVVTLYE FEPAPGTKSA TVINLTDDIA RSMSVVTARI AIVPGRSVIG
VELPNPVREM VYLRESFDHD AFRNTTAQLA IALGKDISGE PVVADLARMP HLLVAGTTGS
GKSVAINTMI LSLLYRLPPE RCRFIMVDPK MLELSVYDGI PHLLTPVVTD PKKAVVALRW
AVREMESRYE AMSKLGVRNI EGYNARMAEM IAAGEKMPRR APAPGEPENV FDLTPSEPTP
LPYIVVIVDE MADLMLVAGK EIEAAIQRLA QMARAAGIHL IMATQRPSVD VITGTIKANF
PTRISFQVTS KIDSRTILGE AGAEQLLGQG DMLYMQGGGR ITRVHGPFVS DSEVEEIVQY
VKAQGAPNYV TAITEEEEEA AAVEDEEGGS GATGDDLYMQ AVNLVVREGK VSVSFIQRQL
QIGYNRAARL VERMETERVV GPANHQGKRE VLLSHAGLSA KRAGV
//
