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Database: UniProt
Entry: A0A0R2QD43_9ACTN
LinkDB: A0A0R2QD43_9ACTN
Original site: A0A0R2QD43_9ACTN 
ID   A0A0R2QD43_9ACTN        Unreviewed;       571 AA.
AC   A0A0R2QD43;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KRO45402.1};
DE   Flags: Fragment;
GN   ORFNames=ABR70_03545 {ECO:0000313|EMBL:KRO45402.1};
OS   Actinobacteria bacterium BACL4 MAG-120813-bin39.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1655578 {ECO:0000313|EMBL:KRO45402.1, ECO:0000313|Proteomes:UP000053569};
RN   [1] {ECO:0000313|EMBL:KRO45402.1, ECO:0000313|Proteomes:UP000053569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL4 MAG-120813-bin39 {ECO:0000313|EMBL:KRO45402.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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:KRO45402.1}.
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DR   EMBL; LIBC01000118; KRO45402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2QD43; -.
DR   Proteomes; UP000053569; 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:KRO45402.1};
KW   Cell division {ECO:0000313|EMBL:KRO45402.1};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}.
FT   DOMAIN          222..422
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         239..246
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:KRO45402.1"
SQ   SEQUENCE   571 AA;  62051 MW;  9536B89A70475E10 CRC64;
     RFSGSGIGKL RQRRAQKLVA EDFEVSESPP FETPLVKDLV QEFEPQQEEF EIELEDFDQI
     TQPIPIIQPV KHENSRPQQL LLSSDVKYEL PPLDLLRGGP AAKGKSKANE AVVAALKQVF
     EQFNVDAQVT GFMRGPTVTR YEVELGNGVK VEAISALSKN IAYAVASGEI RILSPIPGKS
     AVGIEIPNSD REIVALGDVL RSPVSSNDTH PMLIALGKDV EGSFLCANLA KMPHLLVAGA
     TGAGKSSMIN SLVVSVLMRA TPDEVRMVLI DPKRVELTNY EGVPHLIAPI ITNPKKAADV
     LSWVVREMEM RYDDLSVFGF RHIDDFNKAV KAGKVNTPAG SDRVLEPYPY LLVIVDELAD
     LMMVAAREVE ESIVRITQLA RAAGIHLVLA TQRPSVDIVT GLIKANVPSR LSFATSSLAD
     SRVILDTPGA EKLVGQGDGL FLPMGASKPV RIQGAYISER EIEAVVNHVK SQLQPVYRID
     LNAPIKSNVI TDDVGDDLDL LLQAIQLVVS TQFGSTSMLQ RKLRIGFAKA GRLMDLMESR
     GIVGPTEGSK ARAVLINAEQ MPDVLESIQG N
//
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