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Database: UniProt
Entry: A0A011QSQ8_9LACT
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ID   A0A011QSQ8_9LACT        Unreviewed;       791 AA.
AC   A0A011QSQ8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=ADIAL_1776 {ECO:0000313|EMBL:EXJ22754.1};
OS   Alkalibacterium sp. AK22.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22754.1, ECO:0000313|Proteomes:UP000020164};
RN   [1] {ECO:0000313|EMBL:EXJ22754.1, ECO:0000313|Proteomes:UP000020164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA   Singh A., Pinnaka A.K.;
RL   Submitted (JAN-2014) 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:EXJ22754.1}.
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DR   EMBL; JANL01000038; EXJ22754.1; -; Genomic_DNA.
DR   RefSeq; WP_034302637.1; NZ_JANL01000038.1.
DR   AlphaFoldDB; A0A011QSQ8; -.
DR   STRING; 1229520.ADIAL_1776; -.
DR   PATRIC; fig|1229520.3.peg.1739; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000020164; 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:0051301; P:cell division; 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; 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; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:EXJ22754.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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:UP000020164};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          445..642
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          201..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..220
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         463..470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   791 AA;  86685 MW;  F1F5D22E151A2EAC CRC64;
     MARRKKRGRP KKKTHKVAPE LLGFILFFIS LLALGSFGFV GRLFTNIFRL FVGETYAFLA
     IILLAAGVYL LLKGEWPSFK GPKARGAALL YTAWLVFVHS RWVLPVLTDS TNSVTATWQA
     LWPQFTSNSI AGNTGGGMIG AVFFGASYFL FGMAGTYIMI VALVFVGIMI FFQLSYSHLF
     ERIRKTLKSM GQGIRGSFSS FMDQQKKNRK KRKKAPEKKK ASRQKQSGIA EEKTSGEPAQ
     SVSSQGTPKE SYLEGEQTTL EIEGYQDIQE MKQKQTAQKN GLANTSAAEE STEPEEGPVD
     FEIGEEENEA YKLPPVSLLN QLEAVDQSNE YSIIQKNVKK LEETFESFGV SAKVTKANLG
     PAVTKYEIQP ATGVKVSRIV GLSDDLALAL AAKDIRMEAP IPGKAVIGIE VPNTEVSTVS
     FRDIIEGQVS NKEKLLEVPL GRDIAGNVAM ADLAKMPHML VAGATGSGKS VAINGIITSL
     LLKAKPNEVK LMMIDPKMVE LNIYNGIPHL LTPVVTNPKK AAQALQKVVQ EMERRYELFA
     ASGSRNMEGY NAFVKRKNQE TDESLLPLPF IVVIVDELAD LMMVASNEVE DSIIRLAQMA
     RAAGIHMILA TQRPSVDVIT GIIKANVPSR IAFAVSSGTD SRTILDSNGA EKLLGRGDML
     FQPMGANKAT RVQGAFISDE EVEAVVHFVK DQQEANYVEE MIPKDEPQKS AADSEDELYD
     EAVSMVIEMQ TASISLLQRR FRIGYNRAAR MVDEMEMNGV VGPSEGSKPR EVLATAETQA
     AEEGNPEVIN Q
//
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