ID D5EQD8_CORAD Unreviewed; 780 AA.
AC D5EQD8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Caka_0884 {ECO:0000313|EMBL:ADE53906.1};
OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS KCTC 12865 / 04OKA010-24).
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC Coraliomargaritaceae; Coraliomargarita.
OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE53906.1, ECO:0000313|Proteomes:UP000000925};
RN [1] {ECO:0000313|EMBL:ADE53906.1, ECO:0000313|Proteomes:UP000000925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC {ECO:0000313|Proteomes:UP000000925};
RX PubMed=21304713; DOI=10.4056/sigs.952166;
RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Coraliomargarita akajimensis type strain
RT (04OKA010-24).";
RL Stand. Genomic Sci. 2:290-299(2010).
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; CP001998; ADE53906.1; -; Genomic_DNA.
DR RefSeq; WP_013042630.1; NC_014008.1.
DR AlphaFoldDB; D5EQD8; -.
DR STRING; 583355.Caka_0884; -.
DR KEGG; caa:Caka_0884; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_358925_0_0_0; -.
DR OrthoDB; 193150at2; -.
DR Proteomes; UP000000925; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADE53906.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000925};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..368
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 408..630
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 656..774
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 360..401
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 705
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 780 AA; 87814 MW; CB4D463E80C1EF8C CRC64;
MRISTKLTIA FVSTLLVFLA FVGLSRYAIT VVRTQEYRLS RLNNVYQELS NVIIGSRVFH
DRMVGEDAVF HSLLATEQSL EPLKADADAV EAVFVRGVLA RLDEFTEVFE RLVQSKQFLN
SLDRDVREGV HQFGVQSVEM QGTLEKLRTE LVKGERADLK LSSIDDAIHA NALIWGWLNR
AISVIDRDLL LDNDLKRFHE HFDEARRSYE AAFSKLQAHD ELAEIAAYAN YLDSLEAVMH
DLRVVSIEIS VAAKVESESV AILEGHGQHL REMVQRLIER CQAKNLQHTG HLSLMYWLFA
LLLLVGGAGM TIWFSMSISR PLNALSKSFD EIASGNFDQR IDVFGNSELD DLARVFNDMA
DRLSRSYSEV EEQVRKRTRE LQKATMKARK LADAAEEANM AKSAFLATMS HEIRTPLNSI
IGFSDMLQET ELDDEQCSDL EAIRSSGALL LELINDILDL SKIEAGKSNL NAVSLDLEET
VQEVSSLFKH GLRKKGVELE VEFAEDLPQF VTTDKLRLQQ LLNNLLSNAV KFTSKGIIHV
RAWYEDRKEP EGPRYYVAVS DTGIGIPEHK LEEVFQAFTQ ADSSTTREYG GTGLGLAICK
RITHLMGGEI SVVSRAGLGS TFKFYFRDLA KLETKDATEA ETKVKPKDLN FPEGFKVLIA
EDDPTNYKLL DKLLARSGIE NVWARNGVEA IDRVKNEDFS MIFMDLQMPE LDGIEATLRI
RELCKEGRPQ PYIAALTANA LGDSRDACFN AGMEDFITKP VARETIRNAL VRYLDHLEQA
//
