ID A1BJQ6_CHLPD Unreviewed; 814 AA.
AC A1BJQ6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Lipopolysaccharide biosynthesis {ECO:0000313|EMBL:ABL66633.1};
DE EC=2.7.10.1 {ECO:0000313|EMBL:ABL66633.1};
GN OrderedLocusNames=Cpha266_2649 {ECO:0000313|EMBL:ABL66633.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66633.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL66633.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66633.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001074};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the etk/wzc family.
CC {ECO:0000256|ARBA:ARBA00008883}.
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DR EMBL; CP000492; ABL66633.1; -; Genomic_DNA.
DR RefSeq; WP_015961164.1; NC_008639.1.
DR AlphaFoldDB; A1BJQ6; -.
DR STRING; 290317.Cpha266_2649; -.
DR KEGG; cph:Cpha266_2649; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_2_1_10; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000008701; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR NCBIfam; TIGR01007; eps_fam; 1.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABL66633.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..102
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 420..495
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 620..731
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 308..363
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 814 AA; 91546 MW; DE87A66DD1F6F682 CRC64;
MKVEQQTPIK QQEEIERGER EISLEEIFKI VLRRKYGIIL VMALSLFAAI FYHYTETPEY
HAVAVMMIND NKEPTDLLAT VLGSGAAVDN KAVKKDVELI KSMPIAMLAV GELYKSARRD
SLEFFEKRIY RSPVSRFFSQ LNVFTPLNAD QNPPYRALSD EELRRYAVKL NSRITVEAAR
ETNVLKVSVA SPFADEAAYL SNTLCRVYRE ADIDRNSEKY AQANKFIAEM LGDQQKKVGD
ADYALSKYME ANEIYELTGN TQQLLNKLVE ADAKFKSIQA EYNIANNGLA FLEKKLSESD
RAISSQIAKN VSNQLGSIMD EIKGLESEYM QLVQEKGIDN ADVKAKRQQL EVVKTRYEQL
SRSKIAGEIG YAGKAQKFSF DMVSEKLQIQ RKLNELSFSS REFSRLKEYY EGLLGQLPEK
QQDYIKLQRD REVVGKTYLY LKEKLDETRI MLGSEVGGVS VIGSAFVPFK PEKPNLKKNM
LMGLVLGGLL AVLFTYTAEL VDDSVKDDSF FRDIGLATLS IIPLVPGEKN AVPSREVSGF
NRILYNTSKA FREKVLLSGN GAGKRKGAQP KVETPMPMIT DSLSSSFAES FRTLRTALDY
SRVESPLKSL LISGTAMSEG KSTVCSNLAM AYALVGKKTI IVDCDFRRAS QHKKFSVKRE
KGLTDYLFGE DRSIDESYFQ ATHVDNLFLL SSGKKVPNPN ELLGSAKMQD LIRELETKFD
KVIIDSPPLF LSDAAQLAHS IDGILLVSRL QFTSRKPIQD FVSDHFMRPL LLGVALIGSR
QGTGYGYGKY GYGKYGYGKY GYGKYQYGQY EEQA
//