ID A0A199XS12_9FLAO Unreviewed; 816 AA.
AC A0A199XS12;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DNA translocase SpoIIIE {ECO:0000313|EMBL:OAZ04202.1};
GN Name=spoIIIE {ECO:0000313|EMBL:OAZ04202.1};
GN ORFNames=FLB_11950 {ECO:0000313|EMBL:OAZ04202.1};
OS Flavobacterium succinicans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=29536 {ECO:0000313|EMBL:OAZ04202.1, ECO:0000313|Proteomes:UP000093807};
RN [1] {ECO:0000313|EMBL:OAZ04202.1, ECO:0000313|Proteomes:UP000093807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD5b {ECO:0000313|EMBL:OAZ04202.1,
RC ECO:0000313|Proteomes:UP000093807};
RA Poehlein A., Daniel R., Simeonova D.D.;
RT "Draft genome sequence of Flavobacterium succinicans strain DD5b.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OAZ04202.1}.
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DR EMBL; JMTM01000035; OAZ04202.1; -; Genomic_DNA.
DR RefSeq; WP_064715029.1; NZ_JMTM01000035.1.
DR AlphaFoldDB; A0A199XS12; -.
DR PATRIC; fig|29536.5.peg.1258; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000093807; 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 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:UP000093807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..665
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 816 AA; 90715 MW; FAFF495E01DF299A CRC64;
MAKTRKKNTP DSPSDSANPK LQFWKVSKQN KLIIGSLLLL FSIGLLIAFV SYFLHGQEDQ
SAVNAMTDRN EVVQNWLGKI GVFLADALLY KGFGIASFLF VRLFFLTGLF LFLDLRLKRL
KNIWFWDLFL IVILSVLFGF FATSVPELGG TVGYELNLLC QDYIGKTGTL LVLIFGVLIY
LIFKLKVSPE KIQSLFHSTK EEIKDEIANN PFSKETSNAY NLEEFAIEEE EDIEDTIHLK
TSGSQFEINK EALKPTISSA SEINLEPQLK PQPLVTPVRN EVIATNDEAF VIEKAAEEDI
IEENLASRLV SDFGLFDPTL DLSHYKYPTI DLLKEYSTGG ITINQEELEE NKNRIVDTLR
NYKIEIAQIK ATVGPSVTLY EIVPEAGIRI SKIKSLEDDI ALSLSALGIR IIAPIPGKGT
IGIEVPNKNP TMVSMKSVIG SAKFQEAEME LPIALGKTIS NETFVVDLAK MPHLLMAGAT
GQGKSVGLNA VLTSLLYKKH PAEVKFVLVD PKKVELTLFN KIERHYLAKL PDTEDAIITD
NAKVVATLNS LCVEMDNRYS LLKDAMVRNI KEYNEKFKSR KLNPELGHRF LPYIVLVVDE
FADLIMTAGK EVEVPIARLA QLARAIGIHL IIATQRPSVN VITGLIKANF PARIAFRVTS
KIDSRTILDT QGADQLIGRG DLLYTNGNDV VRVQCAFIDT PEVEKITEFI GAQKAYATAY
LLPEFVGEES GINLDIDVSE RDPLFREAAE IIVNAQQGSA SLLQRKLKLG YNRAGRLIDQ
LEAAGIVGAF EGSKARSVNI QDMSSLDQFF NNELNN
//