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Database: UniProt
Entry: A0A0A0BMV2_9CELL
LinkDB: A0A0A0BMV2_9CELL
Original site: A0A0A0BMV2_9CELL 
ID   A0A0A0BMV2_9CELL        Unreviewed;      1323 AA.
AC   A0A0A0BMV2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KGM09833.1};
GN   ORFNames=N869_05940 {ECO:0000313|EMBL:KGM09833.1};
OS   Cellulomonas bogoriensis 69B4 = DSM 16987.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM09833.1, ECO:0000313|Proteomes:UP000054314};
RN   [1] {ECO:0000313|EMBL:KGM09833.1, ECO:0000313|Proteomes:UP000054314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=69B4 {ECO:0000313|EMBL:KGM09833.1,
RC   ECO:0000313|Proteomes:UP000054314};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:KGM09833.1}.
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DR   EMBL; AXCZ01000168; KGM09833.1; -; Genomic_DNA.
DR   RefSeq; WP_052105506.1; NZ_AXCZ01000168.1.
DR   Proteomes; UP000054314; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR023836; EccCa-like_Actinobacteria.
DR   InterPro; IPR023837; EccCb-like_Actinobacteria.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03924; T7SS_EccC_a; 1.
DR   NCBIfam; TIGR03925; T7SS_EccC_b; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 2.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS50901; FTSK; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          459..660
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          819..1009
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1104..1288
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         482..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         837..844
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1121..1128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1323 AA;  141302 MW;  32A768FD36D4A994 CRC64;
     MTAPTVAEPA APPPVPTGKV TVQAPPELAA SEGMSGTLSM MVPMLGSLGG IVFVAVAMPG
     PRGMIGAGMF LIATLGFVGV NIWRQRSQHQ STVVGARREY LAYLTELRGS VRAAARSQRR
     RALWFHPDPR ALAVLAEERS RVWERRPEHD LFLHVRTGRS DQALCVTLEP AETPPLAQLD
     PVAASAAHRF LVSHSTQRDL PHALDLRTAA TVEVAGDEDA ARGTARAVLA QIAAFHSPED
     VRVAVLTTPE AAPAWDWAKW LPHVQSTRAR DAIGPARMIS TSMADLEVLL PEGLQDRPRY
     VPGTPPDGPH VVIVVDGPLP TGHALLSPDG TCGVTVLHLP DRWDELTHPH TLRLVLGGDD
     PLGRADRRAG TALGVARLGT ATPAGTADHM GVADAEALAR RLAPLYLESG PVQTDNQTSA
     ELVDLLGVGD IRDFDPGVHW RPRLQRDRLR VPIGLTSQGQ PLALDIKESA QQGMGPHGLI
     IGATGSGKSE VLRTLVLALA LTHSSEDLNF VLVDFKGGAT FAGMADMPHV SAIITNLSEE
     LTLVDRMQDA LQGEMTRRQE LLRAAGNFAN VTDYEKARTA GRTDLPPLPA LMIVADEFSE
     LLSAKPEFAD LFVAIGRLGR SLQMHLLLSS QRLEEGRLRG LESHLSYRIG LRTFSAGESR
     TVLGVPDAHT LPPVPGMGYL KPDTTSLIQF RASYVSGPPP ARHRSTAGAG GRSGDARIEM
     FTAAPVIGAP VPDGPAPAAV PDTPEDRSTF DIAVERMVGQ GPPAHKVWLE PLVVPATFDQ
     LMPDLAPDPE LGLVSRTWRD AGDLVVPLGV VDRPLEQRRE NLTLSLGGAA GHVAIIGGPR
     SGKSTAARSV VTALALTRTP AEVQVYVMDF GGGTFAPLAH LAHVAGVGTR AEPDVVRRIV
     AEIDGIVDAR EAYFRANGID SIETYRQRRA QGLADDGYGD VFLVVDGWST VRTEFDELEA
     QIQTLAGRGL TFGLHLVATA SRWMDFRTQV KDVFGTKIEL RLGDPMDSEI DRRVAANVPE
     NRPGRALTTT GHHAMVALPR VDGASDGGTL GQGIDHLVRS VAEAWHGPAG PKLRLLPELV
     PLQDVRDMAP TGDRLLLGID EARLAPVGLD PRSTSHLVAF GDSGSGKSAL LRGLAAEVRR
     THTPQQAQIF AIDLRRSLLG EIPEEYLAGY LTTQEQATTS MTELADYIRG RLPGPDVTPE
     QLRTRSWWTG AEAYVLVDDY DLVATSTGNP LLPLLPLLAQ AGDIGLHLVI ARRTGGAGRA
     LYEPVLQALK DLAAPGLVLS GNPDEGALVG KARPTPAPPG RAQLVTRDHG LQVVQLALAP
     SQH
//
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