ID A0A139X1G7_9CYAN Unreviewed; 1022 AA.
AC A0A139X1G7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=WA1_35660 {ECO:0000313|EMBL:KYC38528.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC38528.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC38528.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC38528.1,
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 + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:KYC38528.1}.
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DR EMBL; ANNX02000040; KYC38528.1; -; Genomic_DNA.
DR RefSeq; WP_017745866.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139X1G7; -.
DR STRING; 128403.WA1_35660; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KYC38528.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transferase {ECO:0000313|EMBL:KYC38528.1}.
FT DOMAIN 2..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 481..715
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 717..860
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 897..1014
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 321..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..429
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 338..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 947
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1022 AA; 113780 MW; FD1E925DDAD7F513 CRC64;
MSQDKELEIQ MQFLEEANDY LNTLEGVLLE INSSNRISPE KINAALRAAH SIKGGAGMMG
FRSLSDLAHR LEDSFKVLKT RKNSLEIDTE LQSLLLSGVD WLRQIVELLS EGGEIDEQWL
GTFCYPVFDE LHQRLGDPTP EDAATMLSPE DGQDIVPLLF ETEVEGCLQR LEAVLADGEQ
PCLKEEVAIM AAELGGLGEM LQLSAFSQLC MSIATYIETA EPSQVETVAR SALEAWRRSQ
ALVLTNQLES LPAELQIGEV AYDTVDYTPT ELLEVEPAPV PEVEPEFIEA GVLQPEETEE
SWLDREIIAA DFEALEAAFA EESNAQVEEP EPEPATVSSR EIPTSSYNRK AEQTTGSHKS
ETPENTVRVP SRQLEQINDL FGELIIQRNG MNLQLERLRK LIRSLNQRVQ VLERENQQLR
TAYDKISTQG VMPSGTPLRA LAPAEQPEEL PPPVSENGDR ANGVEGEFDS LEMDSYNELN
LLSQEVMETI VQVQEVTTDI QLSIDDTDQF ARKLTKTSKQ LQRKLTQIRM RPLSDVVDRF
PRALRDLCVE YGKNVQLKIE GANTLIERSI LEALNEPLMH LVRNAFDHGI EDPATRRASG
KTEQGFIEIT ANHLGNRTII SLRDDGRGIS LDKIRTRAIE MGLEPTLLAQ ATDEELLSLI
FEPGFSTSDQ VTTLSGRGVG MDVVRNNLKQ IRGDVKVDTK LGIGTTFTLS VPFTLSVARV
LLIESNRMLL AFPTDVVSEI FLLNEEHIFP MAIGEVLNWQ GTMLSLVRLG RHLEFNCPRY
DNPTLETPPA INASSILIVN QGNQPVAVQV DRCWGEQEVA IRRVEGNIAL PSGFSNCTIL
GDGRVVPLVN ANEMLYWIAT NERVPRTNQL PSSKLKTVFL TPADEKQASL PGNHKGTILI
VDDSINVRRF LALTLEKGGY QVEQAKDGQD ALEKLQSGLK VQAVICDIEM PRIDGYGFLG
RVKSNTDFRD IPIAMLTSRS SDKHRQLAMQ LGARAYFSKP YNEQELLRTL DDIIFPFAGA
AK
//
