ID A0A109LUT1_9SPHN Unreviewed; 542 AA.
AC A0A109LUT1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASS64_09840 {ECO:0000313|EMBL:KWV94129.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV94129.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV94129.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV94129.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
RL Submitted (NOV-2015) 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:KWV94129.1}.
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; LNBY01000017; KWV94129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109LUT1; -.
DR STRING; 499656.ASS64_09840; -.
DR Proteomes; UP000058666; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 127..180
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 302..419
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 2..47
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 185..212
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 351
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 542 AA; 59970 MW; 22F06B8C7399B9C8 CRC64;
MVEILTARLD RSERALRDAE TALESRMKEL YRANQELRLR ENDLARKLEI ESALLLGALS
NAQMATAYGE RDRGFTVSDS AGSILGTPEG EEATLEKLVE AIHPLDRDRI MREGIQFFRD
RTTGVAHRYE HRIIRQDNGE TRWLRWSIKR EPGTEERPSH IVAMVRDITE ERRNERSVRA
LQLRAERRVR ELATLQLELA AAKTQVEDAL NARNRFISEM AHAIRTPLAS LTGGLELLET
YVHEDGAKDL AVAREAAEQL GELASRLIEE AAADDGKHPV LAQDPPAMET PGAAEGIPDR
PRVLLAEDTE SNRYVVERLL AELGCDVTSV ENGAAAVEAV RREGFDLVVM DVMMPIMNGE
QATQAIRALA GPAARTPIIG ATAHSLQSER ERLLAAGMTA CLAKPVRKDA LETAIRTALI
SGRDVRRNEA RFDHELFRRT FSELPSAYRK RMRDAAKTDI TKYASDVLSA VETDAEEALS
KAAHSLTGVA LNIGAIGIVE ELSAYREARR DGEASIEAFR EAVAACLLAV DDLYEALVAT
DQ
//
