ID A0A1E4UXD7_9PSED Unreviewed; 980 AA.
AC A0A1E4UXD7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A7D25_14335 {ECO:0000313|EMBL:OEC34378.1};
OS Pseudomonas sp. 21C1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1843690 {ECO:0000313|EMBL:OEC34378.1, ECO:0000313|Proteomes:UP000094259};
RN [1] {ECO:0000313|EMBL:OEC34378.1, ECO:0000313|Proteomes:UP000094259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21C1 {ECO:0000313|EMBL:OEC34378.1,
RC ECO:0000313|Proteomes:UP000094259};
RA Souza V., Ponce-Soto G.Y.;
RT "Genomic analysis from strains isolated from an enrichment experiment in
RT Cuatro Cienegas.";
RL Submitted (MAY-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:OEC34378.1}.
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DR EMBL; LXJR01000017; OEC34378.1; -; Genomic_DNA.
DR RefSeq; WP_069519580.1; NZ_LXJR01000017.1.
DR AlphaFoldDB; A0A1E4UXD7; -.
DR OrthoDB; 9770795at2; -.
DR Proteomes; UP000094259; 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; cd12913; PDC1_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 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; 3.
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; 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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
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; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OEC34378.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000094259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..461
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 540..593
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 611..831
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 853..968
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 901
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 980 AA; 108438 MW; 04AD48441AA42D19 CRC64;
MPSSSPGYPL RHWIWRVFAQ SALVPLILVE SVLIAVYLFS NSAIRDAQIG HLQQSAVEDL
EAAAVREGQV IDGRLQAIET QVEILRDAAA EALANTAFVP DALERSRHGL TPSGVFYSRS
DDGRAASFYA NSTPVAKQDH AKALRLAQLD PVMRSIRRAD PLVAAVYFNS WDSYNRIYPW
FMTPDQYPHD MNIPAYNFYY LADAAHNPER KVVWTDVYLD PAGQGWMMSA VAPVYRGDFL
EGVVGQDITL NQMLAKIGEL QVPWAGYAML VAPDNNIIAL PRAGERDFGL RELTEYSYAE
AVRREVLKPE DFNLASRPEL RPLLDALQLP GARVQEVSLG GRHQLVAWSD IRQTGWRLLL
VVDEANLFSE TNRLSTRYLH IGYLMIAGLV LFYLLFFAWM WLRSRRLSEQ LAQPMAGIVS
MMRQLGRGDY APAPVVSRIE EMTQLVEAVQ QAGAQLQSSE GERQEAQRIL QLVLEGTTES
LWEVQAEGMT ISLSGRFVKR FGLPAARMSF SEFNLRVHPD DLERIRHLRQ LFASSGEDQF
EAEYRYADAQ GNYVWLLSRG KVMEREAQGG AWRVAGTHVD ITRLKQVEEE LRHASLTAQE
ASKAKSRFLS SMSHELRTPL NAIYGFGQLI EMETQDKPGS QQEADYAREI VNASRHLTSL
VDDILDLSSI ESRRQQLQLQ PVEIGALLNG CAELVLPEVQ QRQLQLQVLA SADTSLYVQA
DVRRVRQVLL NLLSNAIKYN NPHGCITLGY EVRSGCLRLW VEDSGPGLSD AQQAQLFQPF
QRLGRENSSI PGTGIGLVLC RELATLMGGE MGFASALGQG SRFWIDLPGA APPEAMAADT
DQALAVSATV AADVLCIEDS PACLRIVQEA LREWAQVRGV GSVQRALAEL AQSTPNLVVL
DLDLPDGDGL SILQHMRREP HLSGVPVLVI SASADQSVCA EVLDQGAQAC LSKPIDLAEV
RRVAAALLGA AAMSSRASDF
//
