ID A0A1Z4NNP1_9CYAN Unreviewed; 1236 AA.
AC A0A1Z4NNP1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES3974_40150 {ECO:0000313|EMBL:BAZ07352.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ07352.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ07352.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ07352.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; AP018254; BAZ07352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NNP1; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000218621; Chromosome.
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; 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 Kinase {ECO:0000313|EMBL:BAZ07352.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000218621};
KW Transferase {ECO:0000313|EMBL:BAZ07352.1}.
FT DOMAIN 4..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 691..884
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 886..1038
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1103..1220
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 533..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1153
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1236 AA; 137565 MW; 233D1A1CDCBA9491 CRC64;
MITDSSIREQ GYIYFLEEAP ELLQTIEADL FSLAGDFSTA KVHNLMRATH TIKGGAANVG
LEVINKIAHS LEDIFKALYN PDVELDGELQ TLLFQAFECL QLPVTAEISG TSIDADEILQ
RAAGVFAQLQ EKLGDAFGAD TYIPTSEELG FDIVLSIFET GVSQRIDSIA EILENPPGND
ELVDFLQTQG EVFLGLAESL NLPGFAAIAK AMVDALSRNS HRAVEVGNAV LADLLAARAA
VQGGDRVRGG EVSPRLLELA QGVDSSGSDV DSLPLSATTV INTDYHQNQD NQDINIATGE
QELIAPRQNS LRDEIEAFYR FLTQGNHKNY KPIKPTSAKF YLKVIRYILG WFNHELEIPE
SELKLQLLIP IRGIESTLDY LENWLREFFV FLDEFGEGES LRLYRQGVIY TIILALAQFL
DGEPQLIRVL QERIQTLANE YKTYPPITNQ EKNWLDSPKL QALLEVKKYP ASSHSPFSSS
ENREEMMEAI WGENLPANSN SFPNNLVEDL VPENQPIESD SASQQENTII ESTSIPPSPA
INHPHPADST SEEKPTTPRH RSFVRVDVEG LHKLNYLAGE LLIYQKRRSL LDEQLHQVIE
KLFSQLSRHQ NTLNELREIP LQGQSFTSHQ TRNVASVNFD ALEMDEYTEY QLTLHSALEE
SLQLQETAES LDLILRNSIQ VHDKKQILAL NIIDNLVEAR MSPLGNILNR FPQMIQNLAN
LYKKQVEMKL VGTQVLVDKA IAEKLYDPLL HIVRNAFDHG IETPEERLSK GKPETGTIEI
RAYHQGSQTI IEVRDDGKGL NFEKIRQKGL ELGLLTNPQS SEDELVDLLF SPGFSTAGKV
TDISGRGIGL DIVKTQLRAL NGDITLYSRP HQGTTFILKI PFSMTTEQLM LVQAGGATYA
LLLDSIEKIL LPSVTQIREL EGRRVLYWQN GDDEQIIAIR NLAELMHYNS SFVSGASLTH
GTTTLDTQDI DNPILILQNG SELLGLQVDQ IIGEQELVIR PLGNAIAPPK YIYGCTSLAN
GNLILVVDGA LILTSHQMYP PFETYHQPVL SPSKPTALPI SRNETTTAYL ESDNLDSFAG
MEDAGIKLPS LPASEIPLTV PRWVLVVDDA ISLRQTISLT LQKYGYQVIQ AENGIEALEK
LQHHPEISLV ISDLEMPRMN GFELLSHVRQ NPSIKDKPIV ILTSRSAEKH RQLASALGAT
AYLTKPYLEH EFLATVEGIF RENSPSPSQK LLGSAT
//