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Database: UniProt
Entry: U1SDP7_9BIFI
LinkDB: U1SDP7_9BIFI
Original site: U1SDP7_9BIFI 
ID   U1SDP7_9BIFI            Unreviewed;       914 AA.
AC   U1SDP7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ERH30068.1};
GN   ORFNames=HMPREF9244_01357 {ECO:0000313|EMBL:ERH30068.1};
OS   Alloscardovia omnicolens F0580.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Alloscardovia.
OX   NCBI_TaxID=1321816 {ECO:0000313|EMBL:ERH30068.1, ECO:0000313|Proteomes:UP000016519};
RN   [1] {ECO:0000313|EMBL:ERH30068.1, ECO:0000313|Proteomes:UP000016519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0580 {ECO:0000313|EMBL:ERH30068.1,
RC   ECO:0000313|Proteomes:UP000016519};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ERH30068.1}.
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DR   EMBL; AWSI01000037; ERH30068.1; -; Genomic_DNA.
DR   RefSeq; WP_021618476.1; NZ_KE952645.1.
DR   AlphaFoldDB; U1SDP7; -.
DR   STRING; 419015.HMPREF3214_01340; -.
DR   PATRIC; fig|1321816.3.peg.1197; -.
DR   HOGENOM; CLU_001981_2_2_11; -.
DR   Proteomes; UP000016519; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; 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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 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:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000016519};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          525..725
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          263..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         542..549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   914 AA;  98698 MW;  81894F829342290F CRC64;
     MKVLLFIPRV FAQLIRDIFG SSSENSDSRL DASCFLLIIF SVLLIASEWF RVDGVLGRYL
     HILAAGAFGI MSVILPIVFL FIAFRLIRNS NLEAENTRVL SGWFLLVWSI SSVLDVLMVA
     GEPHFSWSAL RSAGGLFGHV LGTPLALGLS KPFAVVIFVF IAAFALLMIT GLHIAEIPRL
     LGMTTADNSA SDDDQFPEDV RVGDETLAFA QGVPAHDGTD EAEQSVRQPW WKKLFNRMRH
     EETDTNLDEY EGDTAFQNPM RVQDDSQTNR QNVRSAQSGR FEPDFGEDET RAIGREAGAN
     APEFSGAAQA AAGRIAGHVP ATSSPQDIAE TMAVAGAGAV GAVAGEVGST RAVPTHSSAV
     APEQSPSQED NESQSGGFEQ LPAPSDNGQT YQKPSLDLLV AGKPHAVRTE ANERVIHALR
     ATFQEFGVDA DVVGFLRGPS VTQYEVELGP GVKVEKVTNL QRNIAYAVAS SDVRILSPIP
     GKSAIGIEIP NIDREIVHLG DVLRSPEALN DNNPMTVGLG KDVEGNFVTA NLTAMPHLLV
     AGATGSGKSS FINSMLTSIV MRATPEQVRL IMVDPKRVEL TAYAGIPHLL TPIITDPKRA
     AQALEWVVKE MDARYDDLQY FGFRHVKDFN EAVLAGKVHA PAGSNRKVAP YPYLLVVVDE
     MADLMMVAKN DVESSIQRIT QLARAAGIHL VLATQRPSVD VVTGLIKSNV PSRLAFATSS
     ATDSRVILDS VGAEALIGQG DALFLPMGKP KPTRVQGAWV SESEIRSAVD FVKTQRKPQY
     RQDIEQMAAQ QDTKQAIDEE IGNDMDDLLQ AAELVVGAQF GSTSMLQRKL RIGFAKAGRL
     MDLLESRGVV GPSEGSKARE VLVQPSQLQE VLGFIRGDAP SIDAAAQAQV EEHHNENSSY
     PSDYDGADTY DNEG
//
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