ID A0A494XM35_9BURK Unreviewed; 1163 AA.
AC A0A494XM35;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D7S86_17495 {ECO:0000313|EMBL:RKP51755.1};
OS Pararobbsia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pararobbsia.
OX NCBI_TaxID=1792498 {ECO:0000313|EMBL:RKP51755.1, ECO:0000313|Proteomes:UP000270342};
RN [1] {ECO:0000313|EMBL:RKP51755.1, ECO:0000313|Proteomes:UP000270342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHC34 {ECO:0000313|EMBL:RKP51755.1,
RC ECO:0000313|Proteomes:UP000270342};
RA Gao Z.-H., Qiu L.-H.;
RT "Robbsia sp. DHC34, isolated from soil.";
RL Submitted (OCT-2018) 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:RKP51755.1}.
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DR EMBL; RBZU01000008; RKP51755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XM35; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000270342; 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; cd00088; HPT; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
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; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000270342};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1163
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019826526"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..845
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 897..1033
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1061..1156
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 964..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 946
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1100
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1163 AA; 125458 MW; E7F4FE2D9D7D6EBD CRC64;
MRRITKWFCH LAVLTGTLGC AAFSCASAPP PGQATRADAF EGRAVVSEWS APATLPALSL
DTMERAALAA HADHLVVGIV PSLSPPLDAS DVRGGVYGMS VDFVEAVGAR LGVPIQWRAF
DDRATMIEAL REHRIDLMTT STFADGPGLL HSRPYVANQM AMIERRARDA DVGVVPRRIA
YVGGIGQARR AHDIALAYPD SVPVAFPGML EALEGVSFGE ADAAIGNLLV ASYLIDQLQL
HNLAPSGYAP IEDGGFDFAL RPDESELVKL IDRGLASLPT SFATGVRGRW AHDVGEPGFV
RPLDLTESER AWIRTHPIVP YTSLADLAPL VFSDSRGEPA GIGVDVLEAI ALETGLTFSG
VLRPNVAEVV QDIASGRALL TPVMADAEDY RHAMTTRIPY MRSLWVIVMR TSSSPLRSID
ALAGKKVALL PDSALWAQLS RAGPGVQLVG ATSVLSAFDA VRDHDVDATL MEISVAHYAL
SLYPKGMFSI TGTVGGAPIP VHLGVRADQP ELASILDKVI AHLPPGEIDA IRRRWLLAGS
PEPKWQQIRP RIIFAAIAGG VGIVLLVVWG VSMRVQIRRR VVAERTLEEQ LAFQLTLLDA
LRRAHDQAEA ANRAKSSFLA TMSHEIRTPM NAILGLIELE LQRSTLAQRR SASLGVIQQA
AHDLLALIDN VLDVSKMDAD KLELAPQAID FYAWIEGLAR LYENLAAQRG LAFRLVEKGT
RRARADVMAD PVRLRQIIAN LLSNAVKFTR QGSVGIEYEI VERTDEVFDV SMTVFDTGVG
IAHADQTILF EPFSQVGDAQ RGTYGGTGLG LSICKRLVDL MDGTLDLDST PGKGTRVTIA
LTLARAVPVA QSIETDEGEA ASLAVQDTRV PERDRGAEED GTPFDIEFAR ATLAGLRVLI
VDDHPANRLV MRQQVELLGC VAAVASDGRD ALGRWSKRRF DVVLTDCSMP LMSGEELSAK
IREREARSGP RTLAPRDIDP NAEGGSPHRC VIIGATANAQ PEARQRALGA GMDECLVKPV
DIPTLVRVLL LARRADVREH AWTSGRHKIE SAIDCVKVAR FGMQRVPFLS SLRGTNIEDK
VAADAALSRS DDRALAALAH RIKGAVRLVG GARLVDACTA LETACSKRPV EIDAIRSAYA
TFCAEFDVFQ ADLEVSIVEA REA
//
