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Database: UniProt
Entry: A0A1Z4NNP1_9CYAN
LinkDB: A0A1Z4NNP1_9CYAN
Original site: A0A1Z4NNP1_9CYAN 
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
//
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