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Database: UniProt
Entry: H7FXC6_9LACO
LinkDB: H7FXC6_9LACO
Original site: H7FXC6_9LACO 
ID   H7FXC6_9LACO            Unreviewed;       760 AA.
AC   H7FXC6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=SMXD51_03903 {ECO:0000313|EMBL:EIA33113.1};
OS   Ligilactobacillus salivarius SMXD51.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1108963 {ECO:0000313|EMBL:EIA33113.1, ECO:0000313|Proteomes:UP000003657};
RN   [1] {ECO:0000313|EMBL:EIA33113.1, ECO:0000313|Proteomes:UP000003657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMXD51 {ECO:0000313|EMBL:EIA33113.1,
RC   ECO:0000313|Proteomes:UP000003657};
RX   PubMed=22582370; DOI=10.1128/JB.00344-12;
RA   Kergourlay G., Messaoudi S., Dousset X., Prevost H.;
RT   "Genome Sequence of Lactobacillus salivarius SMXD51, a Potential Probiotic
RT   Strain Isolated from Chicken Cecum, Showing Anti-Campylobacter Activity.";
RL   J. Bacteriol. 194:3008-3009(2012).
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:EIA33113.1}.
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DR   EMBL; AICL01000003; EIA33113.1; -; Genomic_DNA.
DR   RefSeq; WP_003709828.1; NZ_AICL01000003.1.
DR   AlphaFoldDB; H7FXC6; -.
DR   PATRIC; fig|1108963.3.peg.1478; -.
DR   HOGENOM; CLU_001981_12_4_9; -.
DR   Proteomes; UP000003657; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}.
FT   DOMAIN          426..618
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..214
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         443..450
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   760 AA;  85849 MW;  204F612ED6934120 CRC64;
     MEHYDGPAFF RRQGRSSNID ENSAKKSSNV SSTSSFKKAS HKFEGRNIRR QRAFVRTSTT
     LDSYRTRSFR PTYVPPSSIR FTNKNDKEKY SKLVAKLRLK FNNLWLFTDD FQESKDIVDD
     NIFEENNLQQ IEDKNELPED ELETPADSKL TEEINDDNAD DNIKVNKEQE ISEPTDDEEN
     QGNEETEDIN SNEIEVSEDS MEQNDIDTIS SEESDDNSMD TVIPYETARN YHHEEVEETV
     ELKQQDNAPK KKALDRSLDE IMRQEKNDMQ SHLSLFNQSQ KGDNKENLMY KFPEMSLLPD
     PVINDEDEMD EWVLQEVDIL NETLEAFHVK AEVTNWTIGP TVTQFEVTLN RGVKVNKITN
     LTDDLKLALA AKDIRIEAPI PGKRSVGIEI PNKKSRPVML SEVLNSKVFK EATSPLTVAL
     GVDLFGQPQV TNIAKMPHGL IAGATGSGKS VFINSMLVSL LYKATPAELK LLLIDPKAVE
     MAPYHDIPHL LAPVVSDPQA ATASLKWAVN EMEERFERLA AAGAKNIESY NEKAEENGDY
     GLKMPYIVIV IDELADLMMV ASSEVQDYII RITQKARAAG IHMIIATQRP SVDVITGVIK
     SNIPTRIAFM VSSQVDSRTI LDSSGAERLL GRGDMLYLGN GESQARRIQG TYVEDEIEKI
     TDFIREQGTP TYAFNPDKLK VIETQTENED DLMPEILEYI VNEDGISISK LQRVFSIGYN
     RAAKIIDDLE SKQYISSAKG SKPRDVYLTP EKLEKMKGTN
//
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