ID A0A1U7ITU4_9CYAN Unreviewed; 741 AA.
AC A0A1U7ITU4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES2119_01160 {ECO:0000313|EMBL:OKH40947.1};
OS Phormidium ambiguum IAM M-71.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH40947.1, ECO:0000313|Proteomes:UP000185860};
RN [1] {ECO:0000313|EMBL:OKH40947.1, ECO:0000313|Proteomes:UP000185860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH40947.1,
RC ECO:0000313|Proteomes:UP000185860};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:OKH40947.1}.
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DR EMBL; MRCE01000001; OKH40947.1; -; Genomic_DNA.
DR RefSeq; WP_073591621.1; NZ_MRCE01000001.1.
DR AlphaFoldDB; A0A1U7ITU4; -.
DR STRING; 454136.NIES2119_01160; -.
DR OrthoDB; 415806at2; -.
DR Proteomes; UP000185860; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000185860};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 354..572
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 610..727
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 320..354
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 741 AA; 84753 MW; 095C664D12DA91BF CRC64;
MNKPLRLLLI QDSRNDARLL ANELKRGGYT PIFKRVETLS AIKSALEKAD WDIVFTDYSL
PKFNVLTVLQ LVRKKQINLP VIVLLENISE DLIVTAIKAG AKDCLLKNNL QRVSQIVKRE
LQVDINNKNN PFLIHNSHIK EYQEVALKNQ QKAEREKILN KIIRVLNQRL DTEHILQQIV
QLTGECFSVD RVILYSTKSE QIQVLNEWLA DRRIPSMLKF KVPLSEWPDL LDPNSEFNNG
RAFHAPHYPP FSATDSQQKN IDKFKIRSVL SVPIFIHDRV FGGLVLHTTS SSRTFIDEEI
KLLERIADQA TIALYNALSY EHLEQLVKQR TQELEKAKLE AETANRAKSE FLANMSHELR
TPLNSILGLS QMLQQEFYGK LNSKQKQYMN CIYNSGEHLL SLINDILDLA KIESGKEELM
LESVEIKELC YYCISIVQER AQSKGLILKS EIDPLVSHFI ADQRRLCQML LNLLSNAIKF
TPAGQVSLVV KKEPKGTSFT VADTGIGIAD QDISVLFQPF SQLDGKLNRQ YQGTGLGLVL
TRRFAQLHGG DISVESQRGV GSNFRIYLPD LSLRNFDTNY YQYQEKEEIE LNNCRENILL
LEGQSLQKRP ILLIEEEDKG VKALRNYLEI LNYQVEHLTN VVNFSEQVRL IKPGLIILGV
YLPNDRSGID LLKVLRSQKD LEQIPAIMLT PTLLKDERER CLAAGANDYL VKPLGVAKIE
AILSQYYNRA DYSWLLSTSN R
//
