ID A0A099J3Y2_9MICO Unreviewed; 832 AA.
AC A0A099J3Y2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BJ997_003163 {ECO:0000313|EMBL:MBB5642615.1}, GY21_16605
GN {ECO:0000313|EMBL:KGJ72252.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ72252.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ72252.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ72252.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5642615.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5642615.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:KGJ72252.1}.
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DR EMBL; JPXF01000085; KGJ72252.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5642615.1; -; Genomic_DNA.
DR RefSeq; WP_035838380.1; NZ_JPXF01000085.1.
DR AlphaFoldDB; A0A099J3Y2; -.
DR STRING; 1001240.GY21_16605; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGJ72252.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBB5642615.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 611..824
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 832 AA; 87333 MW; 03DCFB08000C3C55 CRC64;
MKRGRLRVLL GAAPGVGKTY TMLEEGRRLR DAGKDVVVAV VETHGRAATA VMLEGLEVVP
RITVEHRGVE LTDLDLGAVL ARRPDIALVD ELAHTNAPGS VHAKRFQDVE AILDAGIDVI
STVNIQHIES LNDVVEQITG APQRETLPDS VLRRADQVEV VDLAPQALRD RLAEGHVYPA
ARIDAALSNY FRLGNLTALR ELALLWLADE VDTALQAYRT EHGIDSKWEA RERVVVALTG
GPEGETLVRR GARIAARSAG GELVAAHVIS QDGLSAPHPG ALAAQRALVE ELGGSYHQVV
GNDTARALVD FARAANATQL VIGVSRRARL TAALAGPGIG ATIVRESGDI DVHIVTHSAA
GGKFTLPRLG GALSARRRMA GFALAIVGGP LLTWALVLLR STESITSDVL SYQLLVVLVA
LVGGLWPALF AAVLSGLTLD YFFVDPVHTI TIAEPTHAVA LVLYLVNAGL VSYVVDQAAR
RSRTAQRSAA ESALLATVAG SVLRGEDALH ALVTRTREAF RLTAVRLVAG STALASDGEP
GDGPPATTVP VGSRAVLELY GPDLEASERR LLSVIAIQID AALEHTDLAQ TASRIGPLAE
ADRMRSALLL AVGHDLRRPL AAATAAISGI RSTEVELSQA DRKELLATAG ESLETLSALV
TNLLDVSRLQ AGELAISIGP VDLLDIVLPA LDELNLGPDS VELDISPDVS LVLADAGLLQ
RAVVNLLANA IRFSPPGKPA RLAASQFAGT VQIRVSDQGP GIPADRRDDV FVPFQRLGDT
DNLSGLGLGL ALSKGFIEGM HGTLEADDTP GGGLTMVISL PAADTPPSEE PT
//