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Database: UniProt
Entry: A0NKM5_OENOE
LinkDB: A0NKM5_OENOE
Original site: A0NKM5_OENOE 
ID   A0NKM5_OENOE            Unreviewed;       787 AA.
AC   A0NKM5;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   Name=ftsK {ECO:0000313|EMBL:EAV38915.1};
GN   ORFNames=OENOO_64027 {ECO:0000313|EMBL:EAV38915.1};
OS   Oenococcus oeni ATCC BAA-1163.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=379360 {ECO:0000313|EMBL:EAV38915.1, ECO:0000313|Proteomes:UP000003346};
RN   [1] {ECO:0000313|EMBL:EAV38915.1, ECO:0000313|Proteomes:UP000003346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1163 {ECO:0000313|EMBL:EAV38915.1,
RC   ECO:0000313|Proteomes:UP000003346};
RG   Laboratoire de Microbiologie (Universite Bourgogne);
RG   GENOME Express;
RG   UMR Oenologie Ampelologie (Universite Bordeaux 2);
RA   Guzzo J.;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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:EAV38915.1}.
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DR   EMBL; AAUV01000059; EAV38915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0NKM5; -.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   Proteomes; UP000003346; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          444..641
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          214..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         462..469
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   787 AA;  86884 MW;  140B5B8736753ABE CRC64;
     MATRRRRKTK KTQKINSKTI LILVIDALFV LGIFRLGIVG NFFANIYKYV FGNFFVIFIL
     LIAFFLNYWL LYKKLPKIPT RIIVGIIFLA LPFLAISSLF FAADLKSGSN LLRQLFKVTA
     NDMSHNRSQT NVGGGLIGAL LYLSLSQMIS NVGVWIVSIL SAVFGIFRLL DKSVLSSISK
     TTQFCREKVS KIKDNRANKV KDPQSNNFLK KYFQGDDSKE ESRPVSNVAT RTEEVQPKIR
     WNQVDSGNDV DRGTRQSTNF ATDNSLNNST QNSGIANPSN APTDFDDNIS KEIGDDQVID
     SIETVDNPDY KIPPFSVLSH IQIVDQTSEY KQLTKKSQIV RDTLKSFNIE TEVSSVSLGP
     TVTQYELKPA RGVKVSTIAN RADDLALALS AKSIRIEAPI PGKPFVGVEV PNEVQATVGF
     SDIIEHSQFN PKHPLTVPLG RDVNNDVVSA DLSAMPHLLI AGATGSGKSV AINGIISSLL
     MRLKPNEVKL MMVDPKRVEL SMYNDLPHLL APVISEPRKA ARGLQKAVKE MERRYELFAD
     HGVRNIDGWN KKVLDYNKIK GHAMPKMPYI VIIVDELADL MMTAKSDVET AIVRIAQMGR
     AAGVHLILAT QRPSVDVITG LIKANVPSRI AFAVSSGIDS RTILDQNGAE KLLGKGDMLF
     APVGKEPIRI QGAFIPDRDV ETITNYIREE SSAQYASSML VEDGELGDNS SEETGANGEP
     VDDLFNEASD FVIQQKKAST SLLQRRFRIG YNRAARIIDD LEAAGIVGPQ DGSRPREVLV
     SDKKNND
//
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