ID A0A022MM27_9ACTN Unreviewed; 524 AA.
AC A0A022MM27;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
DE Flags: Fragment;
GN ORFNames=CF54_06830 {ECO:0000313|EMBL:EYT83526.1};
OS Streptomyces sp. Tu 6176.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT83526.1, ECO:0000313|Proteomes:UP000020060};
RN [1] {ECO:0000313|EMBL:EYT83526.1, ECO:0000313|Proteomes:UP000020060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT83526.1,
RC ECO:0000313|Proteomes:UP000020060};
RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT cytotoxic benzoxazol nataxazol.";
RL Submitted (MAR-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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
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:EYT83526.1}.
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DR EMBL; JFJQ01000199; EYT83526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022MM27; -.
DR HOGENOM; CLU_001981_9_10_11; -.
DR Proteomes; UP000020060; Unassembled WGS sequence.
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 171..371
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EYT83526.1"
SQ SEQUENCE 524 AA; 56383 MW; 57C1236C7FB6CFAA CRC64;
RPGTPPRVPD LTKTPPAETH DLPPRAEQLQ LSGDITYARP SLDLLERGGP GKARSAANDA
IVDALTTVFT EFKVDARVTG FTRGPTVTRY EVELGPAVKV ERITALAKNI AYAVASPDVR
IISPIPGKSA VGIEIPNTDR EMVNLGDVLR LAAAAEDDHP MLVALGKDVE GGYVMANIAK
MPHILVAGAT GSGKSSCINC LITSIMMRAT PEDVRMVLVD PKRVELTAYE GIPHLITPII
TNPKRAAEAL QWVVREMDLR YDDLAAYGFR HIDDFNAAVR SGKVKSPEGS ERELQPYPYL
LVIVDELADL MMVAPRDVED AIVRITQLAR AAGIHLVLAT QRPSVDVVTG LIKANVPSRL
AFATSSLADS RVILDQPGAE KLIGKGDGLF LPMGASKPTR LQGAFVTEAE VGVVVQHCKD
QMTPVFRDDV VVGSKQKKEI DEDIGDDLDL LCQAAELVVS TQFGSTSMLQ RKLRVGFAKA
GRLMDLMESR NIVGPSEGSK ARDVLVKADE LDGVLAVIRG ESEG
//
