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Database: UniProt
Entry: B8HTN4_CYAP4
LinkDB: B8HTN4_CYAP4
Original site: B8HTN4_CYAP4 
ID   B8HTN4_CYAP4            Unreviewed;       741 AA.
AC   B8HTN4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:ACL46115.1};
DE            EC=2.7.10.2 {ECO:0000313|EMBL:ACL46115.1};
GN   OrderedLocusNames=Cyan7425_3796 {ECO:0000313|EMBL:ACL46115.1};
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC   Cyanothece.
OX   NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL46115.1};
RN   [1] {ECO:0000313|EMBL:ACL46115.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL46115.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA   Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT   "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL   Submitted (JAN-2009) 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; CP001344; ACL46115.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8HTN4; -.
DR   STRING; 395961.Cyan7425_3796; -.
DR   KEGG; cyn:Cyan7425_3796; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_2_3; -.
DR   OrthoDB; 9758283at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL46115.1};
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        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..102
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          380..451
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          535..676
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          223..311
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   741 AA;  81729 MW;  05F0DB62A975EE4D CRC64;
     MQALEDDRID LGKYLTILKR RWLGGAIAFG SILSLVIAYT LLQKPVYQAQ GLLLLKDSEN
     PLASMGATSV GNLVALGGKS SPIDTEAQII RSTPIIQELI TTLQLKDPQG QLLKPEAFLE
     SLSVNNIRGT DLLQVSYRST DPKQAVAIVD LLIKIYKRNN ILANRLETTN SREFIERKLP
     DVTEQLRGLD RQIRSFKETH GIVDLPTEQI ESVKFKSLLA RDLAQAKSLL ATAQARATGL
     SQQVGMSIDL ARFSNAVSQS KGVQVVLDQY QQVEAELAVA RTELQPDHPK IKTLEEQLTE
     LNTILRERVR DVAQASRKGG SLPTSNLQTG ASEQQLVDNF INAEVERLAL SSQVTSLSRT
     EQTYQQRMNA LPKLEQWLGE LERRRVVAQT IYEGLLKTLQ SLQISEQQNA GNVRLIQAAT
     LSDEPVSPKL LLNLILGTIL GSLGAIVVIF ILESKDKTLK SLEEIQQYFD YVTLAMIPFD
     KAAATANKAF KPTQGLERAT PQLYLRDQPN SHLSEAYRTL QANLKFLSSP DHPIRTIVIT
     STRPQEGKST VSANLALAIA ELGHKVLLID ADLRLPLQHQ IWELPNATGL THLLADNHSS
     TKFIHQESDN LDVLTAGPRA PNPLLLLDSQ HMASLIDKFR TVYDYVLIDT PPIGVAVDAL
     VVSKVADGIL VVVRPDVTDS NTANAAREAL VKSNQRVLGL AVNGVTRSDG SYHYYDGYYS
     SDNDTTANGK TRSEKLGMER L
//
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