ID K9RNM8_9CYAN Unreviewed; 727 AA.
AC K9RNM8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ATPase involved in chromosome partitioning {ECO:0000313|EMBL:AFY59078.1};
GN ORFNames=Riv7116_6758 {ECO:0000313|EMBL:AFY59078.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY59078.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY59078.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY59078.1,
RC ECO:0000313|Proteomes:UP000010380};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-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; CP003549; AFY59078.1; -; Genomic_DNA.
DR RefSeq; WP_015122627.1; NC_019678.1.
DR AlphaFoldDB; K9RNM8; -.
DR STRING; 373994.Riv7116_6758; -.
DR KEGG; riv:Riv7116_6758; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_2_2_3; -.
DR OrthoDB; 9758283at2; -.
DR Proteomes; UP000010380; Chromosome.
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:UP000010380};
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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..104
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 377..448
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 536..644
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 180..207
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 727 AA; 80470 MW; D300C2760C4D8146 CRC64;
MESRESVDLD LEKFWYIIKR RWLSAAFIFT ICVGAAAVLG SFKKPVFEAQ GKLLIKKVNQ
TSALTGLGQE IGQLEGLDLK SSPINTEIEV ISSKPILIET IRKLKLKDDE GATLEAKELA
KIINLRAIPA TDVLQISYES KNPKEAGDVV NELMNLYIEN NIQTNRAAAV AAGDFIAKQL
PETQNTVNEA ERKLRQFQQE NNVISLEEES RNAIVIQKEL ETRITETRVT LAEVTARFQS
LQSKIGMNFQ DAINSDSLKS STGVQQVLQN LQQVENDLAI AQTRFFTAHP TVQSLIGRRN
ALQRLLNRRV AQVSNTTGFS RGNLQIGEVT QKLTEELIKS EVETVALKNR LNSLLTALEI
HKQRINRLPK LEQTEKKYER QLETAITTHE NLLQKLQEVR VTENQNIGNA RIIEPAFVAN
KSIKSTKILF LILGGALGTL IATAMIVLLE LKDRSVKTLK EIRKLFGYTL LSTIPSLKKK
SHVHNKDANT LPDIPVRDNP DLPIADAYRM LQANLKFISA DKPLQVIVVT SSVPKEGKST
VSANLAAAIA QLGQRVLLVD ADMQSPLQHN LWGVNNVKGL SDIIVGQVEF ETVVSGGMLS
LDILTAGATT PNPLFLLDSR KMETLIEDFK NTYDFVIIDA PSLVMRADAL ALGKMADGVL
LVARPGILTS ADAATAKEAL ERSGQNLLGM VVNGVIPENE SESYFYYAKD YSDKDNSHPE
PMKTKSF
//
