ID A0A139XA37_9CYAN Unreviewed; 743 AA.
AC A0A139XA37;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Capsular biosynthesis protein {ECO:0000313|EMBL:KYC41551.1};
GN ORFNames=WA1_15985 {ECO:0000313|EMBL:KYC41551.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC41551.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC41551.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC41551.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
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:KYC41551.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANNX02000020; KYC41551.1; -; Genomic_DNA.
DR RefSeq; WP_017746435.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139XA37; -.
DR STRING; 128403.WA1_15985; -.
DR OrthoDB; 580971at2; -.
DR Proteomes; UP000076925; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 25..125
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 536..657
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT REGION 721..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..402
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 721..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82769 MW; FE48E221664CE24F CRC64;
MLKSEKYFHP SLETYAAPLN RADDDDLNLG KVGQALRRRA LLIVGITGVV AAGAVLKAKM
EPPVYKGTFE ILTKPVSGEG RAVANLPQTL GSQGTVSPPE LEESVDTTIA VLQSRGMLEP
VIKKLQDKYQ KKYPDLDLSY ESVLENFIIT PTKQNILEIE YTAPEQEVVR NFLKLVADAY
LEYSLKERQA DINQAILFVN KQVKPIRGRV ESWQDRLRTI RQVNNMVEPA QKSQEVSGHI
ATLTQQQLEN RSMLEQMRAK YFDLQKELAQ EPGEAASNSL LSDNPRYQKI LDQLLQLNAD
ISKRGSVFTD DEEGMKRLNQ QKAASIAFLQ QERQRVNKDF QSRIRELEAR DLSLTEKINN
LNKYVKSLAN INRDYDNIQQ ELKIASENLN QFLAKQQALE IEKAQKQQPW KLLDPKLTTV
RKPEAVSDSA KIYLVMGAVL GSLLGVGAAL VVDKLSNVFY TAQDLKDSTR LPLLGIVPLR
KELGAMAWQE AAGEVQQAAR ASFFEVFRSL YTNILLLGSD TSIRSLVISS PAPEDGKTTV
AVHLALAAAA MGHRVLLVDA NLRTPTIHNL VGLMNIQGLT DVISQDLDWN NVIERSPVED
NLFVLTAGPT PPDPIRLLAS QKMQDLMNQL QSTFDLVIYD TPPLMGFADA NLLAANTNGL
VLTAGLGKLK RTLFQQSLEE LQVSGTPILG VIANKSKDVT TTSYSYYQQY YKKSMSADRV
EDSTNSDFSN FHSTSSGKKT KQE
//
