ID   Q2RFU2_MOOTA            Unreviewed;       545 AA.
AC   Q2RFU2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=ABC-1 {ECO:0000313|EMBL:ABC20697.1};
GN   OrderedLocusNames=Moth_2415 {ECO:0000313|EMBL:ABC20697.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC20697.1};
RN   [1] {ECO:0000313|EMBL:ABC20697.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC20697.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000232; ABC20697.1; -; Genomic_DNA.
DR   RefSeq; YP_431240.1; NC_007644.1.
DR   AlphaFoldDB; Q2RFU2; -.
DR   STRING; 264732.Moth_2415; -.
DR   EnsemblBacteria; ABC20697; ABC20697; Moth_2415.
DR   KEGG; mta:Moth_2415; -.
DR   PATRIC; fig|264732.11.peg.2630; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_2_9; -.
DR   OrthoDB; 9795390at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        489..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        516..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..448
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   545 AA;  60750 MW;  9D979BA6DDAECE7B CRC64;
     MTRHYRYLQR YTEVATVLLR HGWQAYCETR PRRAPARRPL VTGREPGDPV YRHLRLAFEE
     LGPVFIKLGQ LLSTRPDLIP TEMAAEFSYL QDRVRPLAPD VIRQQVFREL GTAPEKAFSY
     FDYQPLAAAS IAQVHKARLP GGQEVAVKVQ RPQLDGVVVT DLAVLENLGR RFKGTVVGRI
     CALEEILATF RRQIERELDF TVEALAMENF RRLYREFPQI VVPRVYWDYT TRGLLTMDYL
     AGKRLSDWYG KGTDCQRAAL LIKALLAPFF QEGIFHGDPH PGNILFLPGG RLGLIDFGIV
     GRLDEDYRYQ AARLILGLQE RDLQAVMEVT LKLGKPMAAV DYQALYEDTA ELVDRVTGMG
     KGDVNLAGLL LGMVELARRH SIRMPGTFFV LGRTIMEGES LARRLDPSLD LVQVSGPLAA
     SYLRSRLRPN PTPGRTYHRA ASTLQDLLEL PRDISRSLDK LARGQLTTIF VHRGLETLYH
     RLDMVSARLS AALIVAALIG AGALILHAGA GPKTGGLSLL GLGVLGGALI LGCLWALLLK
     VGQKE
//