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Database: UniProt
Entry: A0A0M1JK84_9GAMM
LinkDB: A0A0M1JK84_9GAMM
Original site: A0A0M1JK84_9GAMM 
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
//
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