ID A0A101E9P4_9FIRM Unreviewed; 557 AA.
AC A0A101E9P4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=2-polyprenylphenol 6-hydroxylase {ECO:0000313|EMBL:KUK10982.1};
GN ORFNames=XD50_0808 {ECO:0000313|EMBL:KUK10982.1};
OS Clostridia bacterium 41_269.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK10982.1, ECO:0000313|Proteomes:UP000053409};
RN [1] {ECO:0000313|Proteomes:UP000053409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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:KUK10982.1}.
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DR EMBL; LGEZ01000007; KUK10982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101E9P4; -.
DR STRING; 1635275.XD50_0808; -.
DR PATRIC; fig|1635275.3.peg.484; -.
DR Proteomes; UP000053409; Unassembled WGS sequence.
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 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 497..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..557
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 557 AA; 63850 MW; 66C3C49C6314D935 CRC64;
MIKRRYKHIH RLRVIANTFA KHGFGYLLDV LGIRDVLPPF KRFQSDKSHR LSRGERVRLV
FEELGTTFIK LGQVLSTRSD FLPRDIVKEL EKLQDWASPV DFSFVEQIIK EELGGEISEI
FSYFDTKPFA SASIAQVHEA ELLTGEKVVV KVQRPNLKEV VETDLEILFD LARIADRRTS
WGEKYRFTDL VEEFSRSILA EMDFRIEGRN GERLKENFMG DARVYIPEVF WDYSTSKVLT
LERISGIKLS HVDKLAAVGF DKAELAESFA QVMMKQILMD GFFHGDPHPG NVVVLENGAL
GFMDFGIVGC LSPDKKNQLA QIIIALASQN TDLLMHTIFE MGVIPSGVSR RELKADLDKL
RDKYYDKPVE DIKIGDVFND LFDISFKYDI RMPSDFAPLA KVVIITEGVV KQLAPELSIM
KIVEPFARKL IKKQLSPFVL KKNLWGYMLN YIYLLPEIPK LLRGLKERLD EPEVRGVIRH
EGFERLLMKM DQIVNRLSFS IVLLAFSIIM SGLVVAYALS TPKRTVFFDF PIFEVGFIAG
GVLFFWLIIS IIRSGRM
//