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Database: UniProt
Entry: K9PMS3_9CYAN
LinkDB: K9PMS3_9CYAN
Original site: K9PMS3_9CYAN 
ID   K9PMS3_9CYAN            Unreviewed;       699 AA.
AC   K9PMS3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:AFY33827.1};
DE            EC=2.7.10.2 {ECO:0000313|EMBL:AFY33827.1};
GN   ORFNames=Cal7507_3428 {ECO:0000313|EMBL:AFY33827.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33827.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY33827.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33827.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-2012) 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; CP003943; AFY33827.1; -; Genomic_DNA.
DR   RefSeq; WP_015129636.1; NC_019682.1.
DR   AlphaFoldDB; K9PMS3; -.
DR   STRING; 99598.Cal7507_3428; -.
DR   KEGG; calo:Cal7507_3428; -.
DR   PATRIC; fig|99598.3.peg.3881; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_2_3; -.
DR   OrthoDB; 580971at2; -.
DR   Proteomes; UP000010390; Chromosome.
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; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFY33827.1};
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        425..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..126
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          529..677
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          239..266
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   699 AA;  77781 MW;  B66266798DCFD026 CRC64;
     MLKSDKNPYA LSAINISQIS HDVDDELNLG QIATILRRRC LLVAGITFLV ATGAVLKAEI
     DASVYQGTFQ ILTKPVTGEN KAIANLPQTI NTQEETPDKS TAAKTFETTI TVLQSPKVLS
     PVLENLKNQY PSLTYESLIK ELTITSKMSN ILDVKYTNPD QKQVRDVSKL LAEAYLNYSL
     EERQLDVDQA IDFVIRQRQP LEQQVKFWQN KLRDLRLDNN LINPTQKSQE LANQATLLKQ
     QQIENRVQLE QLVARYQDLQ RELAQKPGER AGNSLLSENT RYQKILDYIQ TTDMALKQQS
     AILTDNNPLM VTLKQKKDVL MPLLTQEEVR VQKNLQSRIW ELSARDRSLN EKIKNLNADV
     RNLANITRNH DNIQRELQVA SDALTQFTAK QQALQIEKSQ KQQPWLLLDP KLTTINQPDN
     VSNNAVLMLV VGSILGLILG VSAAFAVDKL SNVFYSTREL KDATKLPLLG IVPLSKQLEA
     ATKQHILSGE KQPCETSFFE VFRSLYTNIL LLGADAPIHS LVISSAGQGD GKSTVAVQLA
     QAAAAMGQRV LLVDANLRAP SLHKGLGAMN MQGLTDVILQ DLDWNHVIER SPLEENLFLM
     SAGPIPPDSV RLLVSHKMRD LMNAMQAAFD LVIYDTPPLL GFADAYLLAT NTHGIILVAG
     LGKLKRTALQ QVLEEIQISG TPILGMIANK SKDSTPQYA
//
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