ID A0A2K8L4M8_9PROT Unreviewed; 971 AA.
AC A0A2K8L4M8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ga0123462_1198 {ECO:0000313|EMBL:ATX82062.1};
OS Mariprofundus ferrinatatus.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921087 {ECO:0000313|EMBL:ATX82062.1, ECO:0000313|Proteomes:UP000231637};
RN [1] {ECO:0000313|EMBL:ATX82062.1, ECO:0000313|Proteomes:UP000231637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP-8 {ECO:0000313|EMBL:ATX82062.1,
RC ECO:0000313|Proteomes:UP000231637};
RA McAllister S.M., Kato S., Chan C.S., Chiu B.K., Field E.K.;
RT "Isolation and genomic insights into novel planktonic Zetaproteobacteria
RT from stratified waters of the Chesapeake Bay.";
RL Submitted (DEC-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 ---------------------------------------------------------------------------
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; CP018800; ATX82062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8L4M8; -.
DR KEGG; mfn:Ga0123462_1198; -.
DR OrthoDB; 5294959at2; -.
DR Proteomes; UP000231637; Chromosome.
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; 2.
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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000231637};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 177..275
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 415..469
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 466..511
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 537..591
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 604..829
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 849..965
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 900
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 971 AA; 108923 MW; 1D8C55845D44BEDB CRC64;
MGNFLKFQAP LWSLLIGVIL SALVFYQVKS WENAHFQHTF EYRADTRTSA IKSVLDHVFE
TADHVVAVIH HELVVERRDE LVSAEIGALA GISDPKNPEV GMLAWLPRLD SADANHHRAP
EYSDFDYQLL MADQNRENWF KPEHLSIPSR WEHMLMAMDT GHHQIDIYTE GDDRHVLVIF
SPVYKRSAAD NPAERREALL GFVVSEWDVA PLIDESLRTM PVGAIDYYLS DASDPQNMPF
YFHSSRTRSG KDQALKTGVS TEKFIVTGEH RWRVRFEAAP AFLQQHQSFT ALQSMGLVLL
LSFMLSGYLW MTTRRTKEIA ETVKQRTAEL HAEKNKLSDS MARYDNLVKS IPVGVYLFRF
YNDDSMGFEY VSPNFCKILG LDADAVLQDG SIAFSAAHHD DLDNLIRANK AAKESLEPFR
WEGRFIINGN TRWVQIESDI TAVDESGSLW SGVVSDITER KKAETKLKTL TKALEYAGEA
AVVTDHDAVI EYINPAFTKI TGYSFEEIVG KKPNILKSSA QDPSFYKVLW DTILRGDVWQ
GTLIDRRKDG TYYPALMSVA PIHDDSGKVT HFVSLQQDMS EYKRLEEQFL QSQKMEAIGV
LVGGIAHDFN NMLAGIVGNT YMAKTRIKDD EKLLGNIEAI ERISMRAAGM IKQLLTFARK
EHVEMSTFSL TNFLNEAIKL AATAIPESIE RSCETSPEEL YIHGDSTQLQ QVIMNLINNA
KDALEGIKNG KISCSLKPYI ADDSFWQRHP NCKGEMFACL TVSDNGGGIP ENVVSKIFDP
FFTTKGVGKG TGLGLAMVYG AIEGHMGAIE VDSVPGEGTT FTIYLPLVDA KPEQEQVSLQ
QAVTGQNELI LVADDEALIL EMYKSVLSHL GYRVIAAHNG EEAVQQFERN MRDISLVVLD
VVMPVMGGMD AAKRIRELDE KLPIIFATGY DRGSLDDAGR EISDHEIINK PFTVESLSQL
IIRSLDTRKQ N
//
