ID A0A013VNY5_9SPHN Unreviewed; 697 AA.
AC A0A013VNY5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein tyrosine kinase {ECO:0000313|EMBL:EXS70177.1};
GN ORFNames=BF95_15740 {ECO:0000313|EMBL:EXS70177.1};
OS Sphingobium sp. Ant17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS70177.1, ECO:0000313|Proteomes:UP000021537};
RN [1] {ECO:0000313|EMBL:EXS70177.1, ECO:0000313|Proteomes:UP000021537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant17 {ECO:0000313|EMBL:EXS70177.1,
RC ECO:0000313|Proteomes:UP000021537};
RA Adriaenssens E.M., Cowan D.A.;
RT "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL Submitted (FEB-2014) 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}.
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:EXS70177.1}.
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DR EMBL; JEMV01000021; EXS70177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A013VNY5; -.
DR STRING; 1461752.BF95_15740; -.
DR PATRIC; fig|1461752.3.peg.2511; -.
DR Proteomes; UP000021537; Unassembled WGS sequence.
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; 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; 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:EXS70177.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..116
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 515..637
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 208..235
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 324..351
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 697 AA; 74762 MW; 5FEC7FDD2D52D4A6 CRC64;
MMTPILTERD LDATPGHGRA ARVTAAARRG WLVLRRHRVI LFVTMALCLL AAVLAILMST
PDYRATASVE IEDVPAGAAG AGTTPRAATD NIEAMMQTEL EVLRSRALAE AVAQDLALVG
TPTFFQRMGH KRPTGGAGSL SQRQVEHDQV VALLRDNLEV ELPGKSRVLR ISFISADPVL
SARVANSYAD NLIRADLKRG FESGVQARRF LLGELDGARR ELARAERELA VYAARLGTEP
GQAAPPSEGT IATRLAQLNG FRAQALADRI AAQKTWESAR RASAETLPEV LSNGAMQTLM
AERAQARAAL VEERQFRKDA HPEMREARAR LAALDDQAQE MANRIRASLK ERYDVAVHGE
TQIAAEIADL ERQGQAAQGR DVQLGIYERS VDTYRMLHDS LLQRYRDMAS QAGFQAGRIQ
PLDRAAVPTK PFSPRIGVTL LLAAIGGLLL GLLLVAARHI FDDAVTSADT LAERVGLPLL
GAVPVTGDNP QPPEIFAPIA SSLLLASAGG LPRSILVTSA QEGEGKSLTL HALALALGRM
GKRVLVIDGD MRRPVQHSLF RLTPARGISE VLTGQASAEE TIIDSSVPGV FLLPCGAVPP
NPAELLATPA LDALLASVRD AYDTVLIDAP PILGLGDTPL LAARVQASLL VVEWGRNHHG
GLRAAVERLR QAGGTLIGAI LTKQQGRMME YDYHRGG
//
