ID A0A1U7IMJ7_9CYAN Unreviewed; 769 AA.
AC A0A1U7IMJ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OKH38435.1};
GN ORFNames=NIES2119_10420 {ECO:0000313|EMBL:OKH38435.1};
OS Phormidium ambiguum IAM M-71.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH38435.1, ECO:0000313|Proteomes:UP000185860};
RN [1] {ECO:0000313|EMBL:OKH38435.1, ECO:0000313|Proteomes:UP000185860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH38435.1,
RC ECO:0000313|Proteomes:UP000185860};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) 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}.
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:OKH38435.1}.
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DR EMBL; MRCE01000008; OKH38435.1; -; Genomic_DNA.
DR RefSeq; WP_073593399.1; NZ_MRCE01000008.1.
DR AlphaFoldDB; A0A1U7IMJ7; -.
DR STRING; 454136.NIES2119_10420; -.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000185860; 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; 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:UP000185860};
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 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..126
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 576..706
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 194..221
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 769 AA; 86254 MW; B3E949FC49602A15 CRC64;
MKIKPYSQPI FPNNGNGKNA QSIPYIYPEP VYEEDNNRIE LRQILGILRR RALVVGSVAI
AVATVIGTRA WNTPPLYEGK FRVLVEPITA ETKVAQNFGA IIYSVLDYGT QTEVLRSPSV
MDAIVKRIQA EYPEVNYGYL MQRLSISRLG DTKIIEVRYQ DSDPKRAEKI LQNIANGYLD
YSRQQRQSDV RQGIDFVKEQ LPNLQERVNT LQARLQKFRQ EYNFIDPEQK AQELGSRIAG
VEQQQIEATT KLNELRSLYT LLQAQLGLQP NEAIVASALS EAPRYQKLLT ELQDIETKLA
TESVRFTEVS PNILALREQR QKLLPLIAQE TQRVVGVAIS PNTINTQKLS NQNSIRLSLT
QQFVDATNQI KVLEVRNQAL KNAENLLVRE FKQMPIRARE YTDLQRELKV TTESLLRFLS
TRENLEIEAA QKATPWQLID APNQSYPISP DKYRNLMLGI VAGLLLGAGA AWLVEMLDNV
FHSVEDLKNQ TGMPLLGVIP FSKALKKAAP GENEAAGLLL PEGEAAITTQ NSGINTRYNA
SQFTESFRSF YTNIRLLSTD MPIRSLVISS STPAEGKTVI SLHLAQAAAA MGQRVLLVDA
DLRRPQIHKR LDMPNMRGLT NLISSEDLDF HEVIQNSPQE ENLYILTAGQ IPPDPTRLLS
SDKMQTLMAD FQSAFDLVIY DTPPLVGFAD ASILATPTDG VILVVGLGKT DRYPLMQALD
TLRISGTPIL GLVANGVKSY TTRWQDTYNR YYHQSSIDRG HSQQMTIDG
//
