ID A0A1B2R0J6_9BORD Unreviewed; 752 AA.
AC A0A1B2R0J6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Tyrosine protein kinase {ECO:0000313|EMBL:AOB30550.1};
GN ORFNames=AKI39_07375 {ECO:0000313|EMBL:AOB30550.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB30550.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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; CP012334; AOB30550.1; -; Genomic_DNA.
DR RefSeq; WP_066634119.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R0J6; -.
DR STRING; 1697043.AKI39_07375; -.
DR KEGG; boh:AKI39_07375; -.
DR PATRIC; fig|1697043.4.peg.1516; -.
DR OrthoDB; 9808257at2; -.
DR Proteomes; UP000093512; 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; IPR005700; EPS_ExoP-like.
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 NCBIfam; TIGR01005; eps_transp_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:AOB30550.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000093512};
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}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..109
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 394..475
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 556..690
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 282..323
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 368..405
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 752 AA; 82430 MW; 663438457E193426 CRC64;
MKQPPLQLEY ANAGGTPPDT PMMSYVDVLL ANRFMIIVVT LLATLVGVAY YLIRPPVYQS
DIAVQVEEEL PTGQRTSMLG DVSSIFDIKQ AASGEMEILR SRLVVGHAVD YYQLYVHATP
DYFPVIGRWL AKRRESFALP TAVTDAIPGG WAWGGERIQL NRIDVPDDLI GKKLRVVALG
AGAYELVDPV HDRRFEGRVG QLERFEVPGG AIEMQIDTLH ARPETSFTVV RESRLEAIES
LQTRMGIFER GRQSNVIGVT LQGQDPVLTA AVLNEIGQEY VRQNTNRKTA QAEKSLAFLD
QQLPVLKKQL EESETRYNAL RNSRGTIDLT EEAKLILGQS VETQNKIFEL KARRQELVTR
FAASHPSIAA IDRQIASLTG DMNKLNSKIR ELPDLEQDVV RLTRDVKVNT DLYTGLLNNA
QQLRMIRAGK VGNVRVVDTA VAAEKPLSPK APIALGVAAL AGLVLGVVAA FLRNALFGGL
TDPDEIERYT GLPVLATVPY SDLQDRLWRR ARRKNARIPA LLAQSNGSTP PIESLRSFRT
VLQVAMRDSS NNIVVFTGPL AGVGKSFLSA NFAFIQAAVG KRVLLIDADF RRGTLNRYFA
TPAENGLFEV LAGTVPLEAV TKRNIMNGVD FISTGRVTFD PSELLASEAF GECLHALAAD
YDIVIVDTAP VLSSSDAAVV GAHAAAVMVV VRSGMNTVGE IRETNKRLQQ AGAPVAGVVF
NGLKLQSEGW GYRSKYGPYR YSRASYYGEN QP
//
