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Database: UniProt
Entry: H2CB11_9LEPT
LinkDB: H2CB11_9LEPT
Original site: H2CB11_9LEPT 
ID   H2CB11_9LEPT            Unreviewed;      1061 AA.
AC   H2CB11;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Cell division FtsK/SpoIIIE {ECO:0000313|EMBL:EHQ08606.1};
GN   ORFNames=Lepil_3956 {ECO:0000313|EMBL:EHQ08606.1};
OS   Leptonema illini DSM 21528.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptonema.
OX   NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ08606.1, ECO:0000313|Proteomes:UP000005737};
RN   [1] {ECO:0000313|EMBL:EHQ08606.1, ECO:0000313|Proteomes:UP000005737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ08606.1,
RC   ECO:0000313|Proteomes:UP000005737};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
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}.
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DR   EMBL; JH597773; EHQ08606.1; -; Genomic_DNA.
DR   RefSeq; WP_002775444.1; NZ_JH597773.1.
DR   AlphaFoldDB; H2CB11; -.
DR   STRING; 183.GCA_002009735_02416; -.
DR   HOGENOM; CLU_001981_9_7_12; -.
DR   Proteomes; UP000005737; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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; 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:EHQ08606.1};
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:UP000005737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          732..924
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          233..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..554
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         749..756
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1061 AA;  117082 MW;  2E81C857384E4780 CRC64;
     MDSASPPASP PPPPPTAGAR IAAALHARSR AVIDDLAVSK RARNVTGFIF IIAGLLSSIA
     AATIDGDAAD LTGRFGIWSA HLLFALFGKA AYLFGPALIW SGLRGIARDD WQAYLSGVIG
     NLSLLWSLAV FFHLSGGTEP GIAGEQFGLL LEFFTGRTGA YTINALLLFT GLLLLLQIPF
     DQVKERVIDM LEGRNRTPDS DSSVWLKRAV ALVPLIPMAY SIYSKFRKSR KEQTTNAQSE
     AKQSSTQETP FSGESVYGEQ NQHSAEPVGK QATSGGTPVL KRFRSEDRPP WIQKVVVSDD
     GLETGSDLEE MTEEAIREAE SLSGRPHEGL EHAGMEQERP FEDRYAQIRR AGGNRWRPGH
     GFDSTEDSEY NPFPDESDDA RPFSNGGDLI IEEDRFPLSS SRNDFKNDLP PSHSSRSGRH
     NPRIVFDPVK NRYLFRQSAE EQALTPTRQR VELLDRMDLD LPHAYKGSFA GEKEAFDNGN
     GLVATDDVAA DSYADGFVDN AGEGSQDDLL QNFDERFEPD SVDNLDETFG DAYSYAGPEE
     TEDLDEEADD FTDEEPAMSA PSVAEANAPK KKADQPLLPN INMPPVVFSE NRFSRYRLSR
     RIVKQTPKVE AEDPEAEIRE NWQRLEKVMS DYGIQAKVVG AIRGPMITMF EVLPEPGVRV
     NRILGIQDEI RMHLAALSVR ILAPIPGKST IGVELPNRNR QYVSMGDLAN GDPEFSSGKR
     ELSIALGKDI TGTNRYLDLT RLPHLLIAGA TGSGKSVFMN SVIGSLLFNH SPDEVRFLMV
     DPKMVELKLF EGIPHLLYPV ITDVRLADRA LNWAVQEMES RYQLLSSAKC RDIRSYNERV
     KSGALSGKLM PYIVILIDEL SDLMMVSAKE VEDSIIRLTQ KARAVGIHVI MATQRPSVDV
     ITALIKANCP ARISFQVAQR TDSRVILDAN GAEALLGRGD MLYKSPTAAD PARMQSPMIS
     DEEIEQLVVE ACRYGHPRFI ELPGRESDDG GGDDGGADVD QALLDSAWEI IQESGKTSTS
     YVQRRLRIGY NRAATIVEKL EQMGYLGPAI GNRPREILKR H
//
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