ID A0A0M1JK84_9GAMM Unreviewed; 739 AA.
AC A0A0M1JK84;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Tyrosine protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TI05_01710 {ECO:0000313|EMBL:KOR33322.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR33322.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR33322.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR33322.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
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:KOR33322.1}.
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DR EMBL; JXSO01000018; KOR33322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JK84; -.
DR PATRIC; fig|1604836.3.peg.1014; -.
DR Proteomes; UP000036918; 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; 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:UP000036918};
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 40..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..116
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 406..484
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 556..717
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 308..400
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 739 AA; 82166 MW; F8517957BD0FF749 CRC64;
MNSKAEVQPN PIAPLSANNH NDEDEINLAE LFSVLWDSKW LISIIAALSF FFGYAYIHIA
TPIYTIDSLI QVPNKPTSGA LAGLSLLGSN FGTQNPIQSE MTIITSRKVI ERVVDKMRLD
IVAIPHYLPL LGASMARRHE DAEEGIAAPP FNLAFYNLKR YAWGGEKITV DTLDIPTKYL
GKKFILIAEE PGFYRIIDPK NNNQTILEGQ VGQTFSYIDD AGTWTVLVSE LNARPGTEFI
LTRNKKLQAI EDLQSQVTID GKKGQDLIGL SLQGSKPKYL LDLLTAIIDK YLAVNEELSS
LSGDEKTLEF FRNELKDVKA RLNIAETRRK NFNLKHRAVD LSSQTSALVQ RIAELENSIF
NMQQKREELI RRFTPAHPTI ATLDTQIAST KRLLAKLNRK TTKLPKTQQK LVNIERDIAI
ANKLYATIIE NLQKLEAAKA TAGGTARVID TPMLPIKPIK PKKKLILALS IVLGLFLGML
LAFILNLFTK IKNPNFIETR FGIPVYAAVP YSKAQKRLTR RGKAPILAAI RPDEAIASLR
YLRNSLFLTV KEAQNNIILV TSSRAGTGKS FVSINLATLL ANADKQVLII DANLHHSSIH
QYFGVKSEPG LLDVITDSVP LEEAIHSNPL ETISLDVLTS GKIVPNASDL LLHEQFSDLL
DQFSKEYDYI IIDAPPILTT TDTAILSSLA GTTLMVLKTN MHSVSEIEDS LKQLNQVGIK
PHSIVFNQVD LKKYGKKYT
//