ID A0A161LM47_9ACTN Unreviewed; 1050 AA.
AC A0A161LM47;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PS9374_01199 {ECO:0000313|EMBL:GAT65566.1};
OS Planomonospora sphaerica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Planomonospora.
OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT65566.1, ECO:0000313|Proteomes:UP000077701};
RN [1] {ECO:0000313|EMBL:GAT65566.1, ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT65566.1,
RC ECO:0000313|Proteomes:UP000077701};
RA Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT Actinomycete.";
RL Genome Announc. 4:e00779-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA Suzuki T., Dohra H., Kodani S.;
RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL Submitted (APR-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 -!- 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:GAT65566.1}.
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DR EMBL; BDCX01000002; GAT65566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161LM47; -.
DR STRING; 161355.PS9374_01199; -.
DR Proteomes; UP000077701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR013587; Nitrate/nitrite_sensing.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAT65566.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000077701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..411
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT REGION 673..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 111572 MW; 07BCE6B27360A821 CRC64;
MGVLGSLLPA NWRVRPRLVA LILLPTVAAV LLTGLQLTTA LSTATEYRRM SEVASLVERL
GVLSHEMALE RDLTAWFIAD QRRPARLVKV REQREVVDRS ATETLKAVAA ISGEHATRVR
TEASQIRRWL HGLPGLRRLI TEGSVLPRAA LGMYSRMIAD FVTLHDDLGR SGGDERLTGD
SLALGALSRA KEQVARQRGI LLVARLEGGF DFDDPADFLG AYRSQVSEVA AFQATASAAQ
NRRFRELVGG PEVDRADATR ALVMSRMREN RSLGTVGIRS WFDSSTAIVD GMRTLERDMA
AAVVARSQEL EGAERRSAMI SGGAILVLLV LILLITAWVA GTLVRPLRRL RSEALEVAGS
KLPETVRVLR ESGDLAPNIE VPSIGVISRD EIGEVARAFD EVHREAIRLA GDEARLRANV
NAMFVNLSRR TQSLVERQID LIDDLEQGEQ DDDRLASLFK LDHLATRMRR NSENLLVLAG
QEQSRRWSEP VPLGDVVRAS LSEVENYERV TLRVEAGTLI IGQAVNDIVH LIAELVENAI
FFSPQDTKVT VTSNGNEMGS VVLAVTDSGI GMSDEELAEA NRRLAEPPAV DLSVSRRMGL
FVVGRLALRH GIRVQLRRPE AGGLSAVVLL PPRVVAQSMR PDPAALAAAA AGRAATPEAD
PFAAGLRQDP FGSAPAGVGA GTRAGAGTGS FGPGHPSFEM SSFGAFQSAE APLAAPSPAE
APPAAPPMPP VRRPGERPPF GMPPMDDTPF GAPPGARPAA GPAPAEAGPA PQAPAGPPPS
VADLWSKPVV SASEVESLWS SPLTPTPAPP SRRPAQPSQP PQPSWQDQPS WQEASAAPEP
SASPASPASP ASPASWQDRS AQPSWQEVSE ADPWSPHRLD PGENTQTLPA VGVSATEPEP
EEFLPIFAAV GSDWFRSSIP ADKTDKPDET AGSGPVEDSG VSGAEHRSAP AAAAERQPWS
STPADQGWAA AEAARKPAEG GLTGAGLPKR VPKANLVPGS APSAPAAPVS PMPPISAERV
RSRLSSFQQG VRQGRAEMNE RSNAAEGEKQ
//
