ID Q1QWU3_CHRSD Unreviewed; 731 AA.
AC Q1QWU3;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Protein-tyrosine kinase {ECO:0000313|EMBL:ABE59065.1};
GN OrderedLocusNames=Csal_1713 {ECO:0000313|EMBL:ABE59065.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE59065.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE59065.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE59065.1; -; Genomic_DNA.
DR RefSeq; WP_011507011.1; NC_007963.1.
DR AlphaFoldDB; Q1QWU3; -.
DR STRING; 290398.Csal_1713; -.
DR KEGG; csa:Csal_1713; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_6; -.
DR OrthoDB; 9775724at2; -.
DR Proteomes; UP000000239; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:ABE59065.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000239};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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,
KW ECO:0000313|EMBL:ABE59065.1}.
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..105
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 381..462
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 552..665
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 269..310
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 355..382
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 731 AA; 80226 MW; B4B23C4FBD9F859C CRC64;
MNLNVPAPQT SKTDNDMELG RILGLLFDAK GLVISLIVLF ALVGAAYAFF ATPIFRADSL
VQVETKTPKN PLADATASAM MPQLPPSRAE MEIMKSRMVL GRAVDLLNLD IRVEPVRVPV
IGGFLQRHQI AAPAFAQDWG YAWGDDHIEL AGMPVAGEYL GKTFTLEVLD ETRYALHYRG
ERLGEGSVGE EASFLGGAVG VEVESIAAAP GATFKLTHAQ RVVAVDQLRD NFGVAEQGNG
TGIISWSLTD PSPALAERVL ATIGDIYVTQ NIQRQSEEAR KSLEFLSKQV PEVRGELAGA
EQQLNAYRSE HDSVDISMET KSVLDRVVNL ESQLNELEFS EAEISRRFTP SHPTYAALLE
KKAQLKRELN TLEERINGMP ETQQEVLRMQ RDVSVNQAIY VQLRNKVQEM QIAEASTVGN
VRVLDDSESF PRPVSPNKIM IIALATILGA AFAVAVVMLR AMFNRGLESP DQLEQLGLPV
YAIVPKSDDQ NRLSRRIRRG GRSQSVPAGL LAWHRPLDVS IEALRSLRTS LHFAMLDSTD
NRLMITGPSP AVGKSFITAN LAAVCAQNGQ RVLVIDGDMR KGQMHKIFKG PSEDGLSEIL
AGRHTLEEMV RPVESIEGLE YLARGVVPPN ASELLASERF TELLAKASER YDLVIVDSPP
VLAVTDATVI GKRVGTTLMV ARFQLNPPKE IELAMRRLDT GGVRVKGAIL NGLERKAATA
YTYGYYNYSY R
//
