TCSB_EMENI
ID TCSB_EMENI Reviewed; 1065 AA.
AC Q9P4U6; C8VPF9; Q5BCD0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Two-component system protein B;
DE EC=2.7.13.3;
DE AltName: Full=Protein NHK1;
DE AltName: Full=SLN1 homolog;
DE Flags: Precursor;
GN Name=tcsB {ECO:0000303|PubMed:12406718}; ORFNames=AN1800;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB07814.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF HIS-552 AND ASP-989,
RP AND PHOSPHORYLATION AT HIS-552 AND ASP-989.
RC STRAIN=FGSC 89 {ECO:0000312|EMBL:BAB07814.1};
RX PubMed=12406718; DOI=10.1128/aem.68.11.5304-5310.2002;
RA Furukawa K., Katsuno Y., Urao T., Yabe T., Yamada-Okabe T.,
RA Yamada-Okabe H., Yamagata Y., Abe K., Nakajima T.;
RT "Isolation and functional analysis of a gene, tcsB, encoding a
RT transmembrane hybrid-type histidine kinase from Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 68:5304-5310(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Nonessential protein which may be part of a two-component
CC regulatory system activated by changes in the extracellular
CC environment. {ECO:0000269|PubMed:12406718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Activation probably requires a transfer of a phosphate group
CC between a His in the histidine kinase domain and an Asp of the response
CC regulatory domain. {ECO:0000250|UniProtKB:P39928}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB07814.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAA64965.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB036054; BAB07814.1; ALT_FRAME; mRNA.
DR EMBL; AACD01000029; EAA64965.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF85586.1; -; Genomic_DNA.
DR RefSeq; XP_659404.1; XM_654312.1.
DR AlphaFoldDB; Q9P4U6; -.
DR SMR; Q9P4U6; -.
DR STRING; 162425.CADANIAP00008448; -.
DR iPTMnet; Q9P4U6; -.
DR EnsemblFungi; CBF85586; CBF85586; ANIA_01800.
DR EnsemblFungi; EAA64965; EAA64965; AN1800.2.
DR GeneID; 2874961; -.
DR KEGG; ani:AN1800.2; -.
DR VEuPathDB; FungiDB:AN1800; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_003731_0_0_1; -.
DR InParanoid; Q9P4U6; -.
DR OMA; MRIPIRE; -.
DR OrthoDB; 27870at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IGI:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IEA:EnsemblFungi.
DR GO; GO:0005034; F:osmosensor activity; IEA:EnsemblFungi.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IGI:UniProtKB.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IGI:UniProtKB.
DR GO; GO:0004673; F:protein histidine kinase activity; IGI:AspGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; TAS:UniProtKB.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IGI:AspGD.
DR GO; GO:0006468; P:protein phosphorylation; IGI:AspGD.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1065
FT /note="Two-component system protein B"
FT /id="PRO_0000032367"
FT TOPO_DOM 28..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 549..849
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 934..1054
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 719..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 552
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:12406718"
FT MOD_RES 989
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305|PubMed:12406718"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 552
FT /note="H->Q: Inactive."
FT /evidence="ECO:0000269|PubMed:12406718"
FT MUTAGEN 989
FT /note="D->N: Inactive."
FT /evidence="ECO:0000269|PubMed:12406718"
SQ SEQUENCE 1065 AA; 117018 MW; C2A70E3B43692143 CRC64;
MRVPIAVQLG LLVLLTALAG LAALAIATWI NNYNFVVDVK SQSLQLVASI KSSQITSNLD
LLETTSKTII TRILIQSALQ RYYAGNTTEE NFASSITDVQ SALGSRGYLS LYQASIYARN
VENGESKARR LLNVTSDEVP EIRLPYDHPN GTAVMLGDEG LGYPPSLYPN LTEDATTNKL
YAFDGVPITT NQPLLLGPLA TNDSFSLISL SLPIINNTSA ADILGYITVV ASAANLQDAM
SSRQGLGSSG QVLLLAPSRP ENRFPTGSRP ATATSEPQIA GLDNQEVRYV FRPTPLPGNK
RRHSPAVASG ASFPLRDYPI ALKVLNQPYD SINHSITDLS SKNENGTRVA VGAIQQRSDL
VEWVLIIEET HGEAFAPVSR LRKIILACVF GTAGVIALLI PPLAHLSVAP IRRLREATRK
SVNPTIGPLS PSLSTMVDPI EISMHNGNEK SEKGGFFNRL KRGRGNLATG HDRDNEPHQF
QIPGRVKERK HIITDELTDL TKTFNEMSDE LVIQYNRLEE RVAERTRELE KAKIAAETAN
ESKTLFIANI SHELKTPLNG ILGMCAVCMG EDDLPRIKRS LQTVYKSGDL LLHLLNDLLT
FSRNQIDQAI RLEEKEFKLS DIRSQLQIIF QNQVQEKQIS FSIKFCHPDT PPINDTPEVI
SRAPGPVYGP PGTAKLKDMV LWGDQHRILQ ILINLVGNSL KFTPEQGTVA IRIKCVGEEK
NPSASPRPES RALSRWRSIG SSHASSRPKT SLDRPRDGGD EETTRPPNLR TLILQFEVED
TGPGIPQHLQ NRVFEPFVQG DLRLNRKYGG TGLGLSICSQ LARLMRGQIQ LNSEQGRGTL
FLVRIPLGFV KESPPSTASS MTSLAGSRTS SVFSLDDLAS VTKAPSNHSV ASQHESTKSN
AEIQDSQPRL VGLSQPFFAP PVPQAKDNGL KKIRALVAED NVVNQEVVLR MLALEDVYDV
TVVKDGQEAY DTVKANMEEG KVFDLIFMDI QMPNLDGIES TRLIRQMGCS APIVALSAFS
EDSNIKDCMN SGMDMFISKP IRRPALKQVL RRFTPIPEEA EKPQM
