ID A0A2W1JNS2_9CYAN Unreviewed; 845 AA.
AC A0A2W1JNS2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cph1_4 {ECO:0000313|EMBL:PZD74990.1};
GN ORFNames=C1752_00550 {ECO:0000313|EMBL:PZD74990.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD74990.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD74990.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD74990.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
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:PZD74990.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQWO01000001; PZD74990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JNS2; -.
DR OrthoDB; 475707at2; -.
DR Proteomes; UP000248857; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248857};
KW Transferase {ECO:0000313|EMBL:PZD74990.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..219
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 223..275
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 301..372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 375..427
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 467..539
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 543..596
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 614..827
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 266..311
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 418..477
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 845 AA; 96739 MW; FDC67194258B9A25 CRC64;
MLDTSYSPSF FIPHGHCYLW KPELVGLHVI SDALVAIAYF SIPCMLVYFV YQRKDLMYSR
VFVLFGAFIL ACGTTHLLEI WTLWNPDYWI SGFAKAVTAI ISVMTAIQLL FVVPQALALK
SPAELEKVNR ALTFSMAERQ RIEAELTDSQ QLFQNAFDYA PIGKALVDLD GSWLKVNSAL
CELTGYSEAE LLQTTFQAIT HPEDLDKDLN YVQHMFLGEI SRYEMEKRYF HKDGQVIWAL
LSVSTVYGPE GHPQYFVSQI QDITARKQYE ADLQILNEDL EARIQERTAD LEQTYIRLQE
SQAEYQDLYE NAPDMYVSVD AESKKILRCN QTLTNALGYT KTEILDRRIF DVYHPACLPD
VEVAFQQFVQ TGRVQDAQLQ LQRKDGSQMD VSLNVHAIRD QQGQVVQSRS SWRDITVRKQ
LERQLQQAKE DLENRVKERT QELLTANQLL QQEVQDRRQA EASLKQSQEQ LELALEASGA
AWWNWDIETG ALNLSPQYFT MLGYTDQQGK GNYLTWENLV HPDDLPWVQN ILAAHLKDAS
TPYAFDYRML TESGAWKWIA NLGKVVERDG QNQPSRMAGV HLDISDRKAV EEELHQLNHE
LSRSNQELGQ FAYVASHDLQ EPLRKIKSFT ELLFKRYPGE GDEKAERYMN HIMDGTSRMQ
VLIRDLLTYS RVGRAELNVQ PTDLNTILAD IQSDLTHIIT ERQVQIESQP LPTLPADPSQ
MRQLFQNLVS NAIKYCQAEI PKIQIRAVQS DAIWTFSVQD NGIGIAPEYA DRIFIIFQRL
HNREAYSGTG IGLAVCKKII ERHGGKIWLS ESSEPGATFM FTLSTQRKLD SHHQEVTLAA
VEVSA
//
