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Database: UniProt
Entry: A0A062X2V5_9LACO
LinkDB: A0A062X2V5_9LACO
Original site: A0A062X2V5_9LACO 
ID   A0A062X2V5_9LACO        Unreviewed;       720 AA.
AC   A0A062X2V5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=Lani381_1797 {ECO:0000313|EMBL:KDA45103.1};
OS   Ligilactobacillus animalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA45103.1, ECO:0000313|Proteomes:UP000027129};
RN   [1] {ECO:0000313|EMBL:KDA45103.1, ECO:0000313|Proteomes:UP000027129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA45103.1,
RC   ECO:0000313|Proteomes:UP000027129};
RA   Sturino J.M., Rajendran M., Altermann E.;
RT   "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL   Submitted (APR-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:KDA45103.1}.
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DR   EMBL; JMHU01000029; KDA45103.1; -; Genomic_DNA.
DR   RefSeq; WP_035449256.1; NZ_POVP01000003.1.
DR   AlphaFoldDB; A0A062X2V5; -.
DR   PATRIC; fig|1605.9.peg.1765; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000027129; 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   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:SF42; DNA TRANSLOCASE SFTA; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}.
FT   DOMAIN          387..579
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          456..483
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        28..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         404..411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   720 AA;  78427 MW;  6BC37FC841049755 CRC64;
     MEHYDGPAFY RNNGRPATKA RVQTKVPAKT EKTPTRTATS NQKECLNESP RAFSPRQVPR
     SLVADRIVKK RPDYDKLVRS LKKAPEDYLL FEGTVLLGTQ AIDLTVKRPL ISDSTETKLP
     KRPTVSSQLK TPTLASDSQT TSSSLATSES LDDSTSQVYL ASSTSQLQSS VSDTHAQSTS
     PANSEAKSVS QSQVTSELTS QVELTSEVAT KSEPQKMTGL KAALAHESSL TQSQPSVTAQ
     PTIPEYEPKH YQFPPLNLLP APVIDDDPAL DDWVASQVQT LNETLKAFHV DATVSDWTIG
     PTVTQFELTL GRGVKVNKIT NLNDDLKLAL AAKDIRIEAP IPGKSSVGIE IPNKTSRPVM
     LSEVLRSDKF QEASSPLTVA LGVDLFGEPQ ITDLQKMPHG LIAGATGSGK SVFINSLLVS
     LLYKASPSEV KLVLIDPKAV EMAPYHDLPH LLAPVISDAK AAAAALKWLV NEMEERYQRL
     AAAGARNLEA YNEKAKAAGE YGLQLPYIVV VIDELADLMM AASSEVQDHI ARITQKARAA
     GIHLLVATQR PSVDVLTGTI KNNIPTRIAF MVSSQVDSRT ILDTAGAERL LGRGDMLYLG
     NGSGQPTRLQ GTYIEDEVDL VTDFVRQQGK PKYAFDPDSL KKRAVESEKQ DDLLPRVLDY
     IVNEETISTS KLQRVFSIGY NRAAAIIDDL EAKQYISPAH GAKPRKVFLT QEGLNKLRSV
//
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