ID H0JV07_9NOCA Unreviewed; 830 AA.
AC H0JV07;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AK37_17690 {ECO:0000313|EMBL:EHK82103.1};
OS Rhodococcus pyridinivorans AK37.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1114960 {ECO:0000313|EMBL:EHK82103.1, ECO:0000313|Proteomes:UP000005064};
RN [1] {ECO:0000313|EMBL:EHK82103.1, ECO:0000313|Proteomes:UP000005064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK37 {ECO:0000313|EMBL:EHK82103.1,
RC ECO:0000313|Proteomes:UP000005064};
RA Kriszt B., Tancsics A., Cserhati M., Toth A., Nagy I., Horvath B.,
RA Tamura T., Kukolya J., Szoboszlay S.;
RL Submitted (DEC-2011) 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:EHK82103.1}.
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DR EMBL; AHBW01000051; EHK82103.1; -; Genomic_DNA.
DR RefSeq; WP_006553473.1; NZ_AHBW01000051.1.
DR AlphaFoldDB; H0JV07; -.
DR PATRIC; fig|1114960.4.peg.3610; -.
DR Proteomes; UP000005064; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR005561; ANTAR.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF03861; ANTAR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01012; ANTAR; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50921; ANTAR; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 119..173
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 365..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 631..747
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 757..818
FT /note="ANTAR"
FT /evidence="ECO:0000259|PROSITE:PS50921"
FT MOD_RES 680
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 830 AA; 90495 MW; 0F1007FA6AF0AA1D CRC64;
MRATAESGEA WSAERLFAGP GECLERFRKT DWSATPLGPV ESWPAELRMA VRTVLPSEVP
MLLWWGPQLV QIFNDAIIPV LGDKYPAAVA QPAPECWHEV WDEVGARVER AMAGTATFAE
EELLFMQRHG YEEETYWTFS YSPIRDESGK VAGVFVATTD VTSRVLGERR LEALSRLGTV
AITDSGRSVI DTCRNALDAL APSHQDIPLA ALFLDSRVVD PDDPQPNWKQ LAVIGTKPGF
SGALLGPDED QLLSKAARAS EPFVVSGVAE RSPDLLDPQR ALGDHPIGTL LLVPLTASGH
DFPLGVLAVG LSPYRVFDAA YSTFVDLVVT KISGLLRDAS AMDAERRRAD AFAALDAAKT
RFFESISHEF RTPLTLLLGP LQSVLDEATA LTDPQRHSLE ASQRAAVRLR RLVDALLEVT
RAETDPSSKP LEPTDPAALT AECVDLFADA AHRAGLDLRS RIADAAAEQT QLDPQTWAHI
VLNLLSNAIK YTPSGSVDVD LDVEGDRLVL KVADTGVGIP ESELGRVFER FHRVESVGGR
SQEGIGLGLS LVRDWVRALG GDATVSSELG RGSTFTVSVP RVVGPPSESP AGTVPGDLGA
LYVAETQQWD RETIAETDST TKKKGGESLP RILVIEDNAD MRDYLTQLLR RQNWHVDAVG
DGDTALERIW SRPPHLVLSD IMLPGRDGVE LLEEIRRDPA TSRLPVILLT ARAGAEATIG
GLRTGADDYI TKPFHPDELV ARVRVNLELS WLREQMLVAR ERESDQLKTA LETRSTLSKA
VGLMMATFKC DADAAFDKLV AFSQHRNVKV REIAEQIVGD YTVSLSDSSR
//
