ID A0R398_MYCS2 Unreviewed; 839 AA.
AC A0R398;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MSMEG_5395 {ECO:0000313|EMBL:ABK75585.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75585.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK75585.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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};
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DR EMBL; CP000480; ABK75585.1; -; Genomic_DNA.
DR RefSeq; YP_889636.1; NC_008596.1.
DR AlphaFoldDB; A0R398; -.
DR SMR; A0R398; -.
DR STRING; 246196.MSMEG_5395; -.
DR PaxDb; 246196-MSMEI_5247; -.
DR KEGG; msm:MSMEG_5395; -.
DR PATRIC; fig|246196.19.peg.5259; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK75585.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..839
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 839 AA; 89056 MW; 26178740CA54380C CRC64;
MTTRASNASK RGELRIYLGA APGVGKTYAM LGEAHRRLDR GTDLVAAVVE THGRKNTAEL
LAGIEVIPPR YIEYRGGRFP ELDVPAVLDR KPQVVLVDEL AHTNTPGSKN AKRWQDVDEL
LNAGITVIST VNVQHLDSLN DVVAAITGIE QQETVPDEVV RSADQIELVD ITPEALRRRL
SHGNVYAPER IDAALSNYFR RGNLTALREL ALLWLADQVD AALAKYRADN KITALWETRE
RVVVAVTGGT ESETLVRRAF RIASKSSAEL MVVHVVHGDG LTGISAAQMG KVRELAVSLG
ATVHTVVGDD VPTALLDFAR DINATQLVLG TSRRSRWARM FDEGIGATVV QQSQKIDVHM
VTHEAAKRGF RWSSTSPRQR HAASWAAALM VPSLICAFSV AILDPFLDVG GKSALFFVGV
LVVALLGGVA PAALSAVLSG LLLNYFLTSP RHTFTMSDPD SALTIVVLLA VAVAVAALVD
GAAKRAREAR HASREAELLA LFAGSVLRGA DLTALLERVR ETYAQRAVSL LRETSDGATI
VDCVGQDPCD RVAAADTAVE AGDEFWLLLS GRELPARDRR VLGAVANQAA GLVRQRELTE
EAAKANAIAK ADELSRSLLS AVSHDLRTPL AAAKAAASSL RSCDIDFSAE DTAELLATIE
ESVDALTALV GNLLDSSRLA AGVIHPELRP VYLEETVQRA LLGIRRGPTG YGRSAVDRVK
VEVGDSVALA DGGLLERVLA NLIDNALRYA PDGLIRVTAG RVANKVLIAV VDEGPGIPRG
AEDALFAPFQ RLGDTNTTTG VGLGLSVAKG FVEAMGGTIS AGDTPGGGLT VEIELAVPA
//