ID M1P278_BARAA Unreviewed; 821 AA.
AC M1P278;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BAnh1_00270 {ECO:0000313|EMBL:AGF73920.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF73920.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF73920.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF73920.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
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; CP003123; AGF73920.1; -; Genomic_DNA.
DR RefSeq; WP_015397429.1; NC_020300.1.
DR AlphaFoldDB; M1P278; -.
DR STRING; 1094489.BAnh1_00270; -.
DR KEGG; baus:BAnh1_00270; -.
DR PATRIC; fig|1094489.3.peg.31; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_018130_0_0_5; -.
DR OrthoDB; 9797304at2; -.
DR Proteomes; UP000011729; Chromosome.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43047:SF72; PHOSPHOTRANSFERASE RCSD; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGF73920.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AGF73920.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 599..816
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 821 AA; 93070 MW; F8A6C4AFD90B6A87 CRC64;
MPSFGDYDPK EKIMKVTQIC VSIFCYLSLL SPAYAAAHSP ALQLPPTLAL PDGLWLILAL
SGGISCAFIF TSIVVILSTK RAARRSLKMI QANFSEKLRH YEWLLEETEQ CLLIWENPTD
LPRITGNVPV LEKAGINQKN FQYFELWLEE TSAQQLEQAL TRLRYNSCPF ELSITAKHKI
LLQVTGVIAG TAAIARFQNI SAQQNENSRL QKDFTRIFAK LKIQENLLDH IQEPVWIQDG
EGKICFMNRI FREMTTTQEG NNDLISLFNG ATQRETDKKE AVFQDYIHTV IGGERRYFHL
TRIMTEEGTA TFARDESTYK NLANEIKHIL KSHYETLDQI STAVAIFDAN QKLKFCNHAF
KVLWPLESTF LENEPSHTLF LERLREEGLI GEHPDWRAWK EELFRASQQT EPNQQIWNLP
DGRTVHVISR PHPQGGITWL YENLTEKIDL ERRYNTLIKI QGETLDKLSE GVVVFGADGR
LRLSNPALSK LWSLPYNLLV EGIHITQLQA HCSTLMIGKE WDKFAQFVTG FSEKRDTCSG
RIDLKNGTII DYTLVPLLDG QTMLTFVNVT DTVHIARALQ EKNEALESAD RLRNEFVQHV
SYELRTPLTN IIGFSDILRD QIFGSINERQ HEYLGYIHSE SGTLLNIVND ILDLATLDAG
IMELNIKPVD IAEAMAQAAA RVEERLNGRH IVLLQKISPS LNFIFSDAMR LHQIFVNILS
NAANFATEGS TIEFHADMQG DDIVFSVHNE GSDIPNDVLD RIFKRFSSHA HHGGRAGAGL
GLSLVKSFVE LHNGRVEILT GTGQGTTVKC FFPGQKENKV F
//