ID Q57D91_BRUAB Unreviewed; 945 AA.
AC Q57D91;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BruAb1_1044 {ECO:0000313|EMBL:AAX74393.1};
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX74393.1, ECO:0000313|Proteomes:UP000000540};
RN [1] {ECO:0000313|EMBL:AAX74393.1, ECO:0000313|Proteomes:UP000000540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941 {ECO:0000313|EMBL:AAX74393.1,
RC ECO:0000313|Proteomes:UP000000540};
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74393.1; -; Genomic_DNA.
DR AlphaFoldDB; Q57D91; -.
DR SMR; Q57D91; -.
DR EnsemblBacteria; AAX74393; AAX74393; BruAb1_1044.
DR KEGG; bmb:BruAb1_1044; -.
DR HOGENOM; CLU_000445_114_51_5; -.
DR Proteomes; UP000000540; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18160; REC_CpdR_CckA-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; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; 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; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAX74393.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAX74393.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..212
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 432..505
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 574..797
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 825..941
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 876
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 945 AA; 103190 MW; D493F02BC05E595E CRC64;
MRPKWCKTTV LASFPRGSAC TARQLKHSAN RIYLDARASV PARRAGILNE DRIELPDDAI
GASAERRSTR DLRKPSRAGI QHERAVGLMS RQTDNTYPKP LVMPKRGPSA ALRLLIVGIL
LMGAAFIYFL FRDQLGDGFA LVLMGVLSMV GVFYLFGAAT GLIQFSQRSD HQDLAHSFMD
TQPEGTVISD PRGQIVYANQ AYARMTGATD ADGIRPLDQV LASEPAASDA IYRLTNAVRD
GLSAQEEVRI SGGLSRGANG SLAPVWYRIK ARALEGGAEF KGPLVAWQVA DISEERAEQE
RFFQELQEAI NHLDHAPAGF FSANPAGRII YLNATLAEWL GVDLTQFTPG SLTLNDIVAG
SGMALIKAVK AEPGTSRNTV IDLDLIKRNG QSLAVRFYHR VQTARDGMPG TTRTIVLDRA
EGDDSSVAQR SAEVRFTRFF NSAPMAIAAV DAEGHTLRTN ARFLDIFSGV VDRDAIDRRV
KLENVVHERD RETFNKALAA AFAGQASISP VDTVLPGNEE RHIRFYMSPV TDLGGEAAEE
AAVISAVETT EQKALENQMA QSQKMQAVGQ LAGGIAHDFN NVLTAIIMSS DLLLTNHRAS
DPSFPDIMNI KQNANRAASL VRQLLAFSRR QTLRPEVLDL TDVLADLRML LARLVGKDIE
LKIDHGRDLW PVKADLGQFE QVAVNLAVNA RDAMPEGGQI TLRTRNIPAA DAAKLHYRDL
PEADYVVFEV EDTGTGIPAD VLEKIFEPFF TTKEVGKGTG LGLSMVYGII KQTGGFIYCD
SEVGKGTTFK IFLPRLIEEK RADDAPVAAK EKKVEKATDL SGSATVLLVE DEDAVRMGGV
RALQSRGYTV HEAASGVEAL EIMEELGGEV DIVVSDVVMP EMDGPTLLRE LRKTHPDIKF
IFVSGYAEDA FARNLPADAK FGFLPKPFSL KQLATTVKEM LEKQD
//
