ID A0A017HDV8_9RHOB Unreviewed; 975 AA.
AC A0A017HDV8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Lokhon_01493 {ECO:0000313|EMBL:EYD72692.1};
OS Limimaricola hongkongensis DSM 17492.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD72692.1, ECO:0000313|Proteomes:UP000025047};
RN [1] {ECO:0000313|EMBL:EYD72692.1, ECO:0000313|Proteomes:UP000025047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD72692.1,
RC ECO:0000313|Proteomes:UP000025047};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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:EYD72692.1}.
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DR EMBL; APGJ01000004; EYD72692.1; -; Genomic_DNA.
DR RefSeq; WP_017928974.1; NZ_KK088650.1.
DR AlphaFoldDB; A0A017HDV8; -.
DR STRING; 1122180.Lokhon_01493; -.
DR PATRIC; fig|1122180.6.peg.1475; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000025047; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR013656; PAS_4.
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; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EYD72692.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000025047};
KW Transferase {ECO:0000313|EMBL:EYD72692.1}.
FT DOMAIN 1..73
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 240..294
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 295..365
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 368..420
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 458..681
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 701..817
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 857..968
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 820..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 751
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 906
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 975 AA; 105744 MW; 3A029F986E76E302 CRC64;
MSVDVSAIFE TVPSAYMLLD RELRFVWGNR KYWEVTGRQP DQVLGRVVTE AFPAEGEAAR
MLNASFERVF ETGRADHLPL IPYPIAGPDG RIEQRYWSAT HTPILDAEGR VEYVLQNTHD
VTDLYMKAHR DDAADMPSGA TGDGGDVLLR AETVAQQNLE LGLATRFFET VFDQAPSIIA
IHSGPDHVIR LANREYRRIA GTHRKLIGRP AAEALPELHE QGFVQLLDEV YDSGEAVTMH
GVQAFVQTES GPASEIHVDF VYQPLAGPHG KTVGILVQGH DVTAQKRAEA ELRAAEERFR
TMAQTMPSHV WTARPDGGLD WVSDQVYDYT GTRGDEILGH NWGHAVHPED IGRVAPIWAA
AIERGSTYEA EFRLRDAAGG YRWFLVRAVP VRDAEGRVAQ WIGTNADIEG RKATEAALAE
LNATLEERVE SRNRALEEIN ATLRQSQKME AIGNLAGGVA HDFNNLLQAI TGSLQLAQRE
LPDGAPAAWR IEQAMGAVER GATLAAQLLA FGRRQPLEPR AVDLGRMIGD IDPILRSAMG
EGVRIETRVA RGLWNTLVDA TNLENALLNL VVNARDAMEG QGRLVIDMVN TEIDARTARS
MTDVVPGEYV RLSVVDEGSG MAPEVIEKIF EPFFTTKPEG RGTGLGMAMV YGFVKQSGGH
VTIESAPGQG TAVRIYLPRS LRSEEPAAQR SAGPVVGGDE TVLLVEDDDD VRLVAGEMLR
HLGYAVIEAE DADAGLAVIE AGHDFDLLLT DVVMPGRLTS REMAERAQAL RPGLPVLFAS
GYSRDAIVHD GRLDEGIQLL SKPYRRETLA RRLRELLDGA ERAEPQAAPR PAPGPPPPAD
AEADAAASGP GDLTGLRVLV CEDDTFIRLD LVEMLTAAGA EVREAATGAQ ALALLQEAPA
DRLLVDVGLP DCSGLDVARE AVARQPDLPV IFATGRDKVP GAEDLPQARV LTKPFGQAAL
LKAVTRGHPA RATAE
//
