ID A0A401ILN0_APHSA Unreviewed; 845 AA.
AC A0A401ILN0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AsFPU1_3598 {ECO:0000313|EMBL:GBF82170.1};
OS Aphanothece sacrum FPU1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=1920663 {ECO:0000313|EMBL:GBF82170.1, ECO:0000313|Proteomes:UP000287247};
RN [1] {ECO:0000313|Proteomes:UP000287247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FPU1 {ECO:0000313|Proteomes:UP000287247};
RA Kanesaki Y., Yoshikawa S., Ohki K.;
RT "Physiological properties and genetic analysis related to exopolysaccharide
RT production of fresh-water unicellular cyanobacterium Aphanothece sacrum,
RT Suizenji Nori, that has been cultured as a food source in Japan.";
RL Submitted (MAY-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};
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:GBF82170.1}.
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DR EMBL; BDQK01000016; GBF82170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ILN0; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000287247; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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 PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GBF82170.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000287247};
KW Transferase {ECO:0000313|EMBL:GBF82170.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..301
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 385..612
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 638..754
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 347..385
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 687
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 845 AA; 97364 MW; 8B648058AFA3A192 CRC64;
MTESSSHQMP YFPLRISLLI GGGLSAIAAL MVGYIELSIQ QTKFQTQALQ LRQYLQYHLN
DYTEVTRTVG HFYEASDEVT QKDFERFSRP FLENYPGIMG MTWAKRISIE ALNTKKKPLK
DNDFSNFNIA TKNDQNTVEK LDKFPIIYEE LKQNNQQIMG LDLGANLLSR VALEKARDSG
KITTSGPIEL TNGDRGFAIY YPTYSPGFFP KNLSESRQEL RGIIYTLYDI KQIFNNTLNK
LEKKELSFYI IDLQAKDNQG ILFSFDKKPE INQSLELPLS CRILFECKKI LTVADRQWSL
VILPDIKLLP IIAKALATFI LVLSLTGILI VYFWKIIDNK NKIEQLIKQR NAELVKTKEY
LEKLIEESNI QLQEAKQKKT ELLGQMSHEL RNPLNILLGF LEVFKREQTL TPEQQDNLAI
MCRSGEYLRS LFNNILELSK LEIGNISLKA TTFNLRDLIN WVIEMFRLKA TGKNLQIMIY
IDPDVPQYIK TDDNKLRQIL INLLDNAIKF TDQGSVTIRL ASDNQDWNLE DNTNDWQPQQ
ILFFAIEDTG RGIALENQVK IFEPFVREHE RDGAGLGLAI TEKLVNLMGG NIQVKSQLNK
GTLIHFNIGF NLPEESEIPT RQSRYNVIGL APNQPEYRLL VVDDQRENRQ LLIKLLRPIG
FQIKEGENGQ EAVEICKNWQ PNLIFMDTRM PIMDGYEAIE KIKALTQINQ PVIITITSES
REAQKNKRSA TIGDDILRKP FEIQRVLDKL VTHLGVSYRY ESQAIEAVEQ DQESVVLNRE
SLEVMSSDWI VQVQGAANAG DGQRLYQLIE EIPEQHYFLI QSMIELVNNF DYRQIRKLSQ
PNIND
//
