ID A0A078KZ90_9GAMM Unreviewed; 912 AA.
AC A0A078KZ90;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_2 {ECO:0000313|EMBL:CDZ77043.1};
GN ORFNames=BN59_01322 {ECO:0000313|EMBL:CDZ77043.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ77043.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ77043.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CCSB01000001; CDZ77043.1; -; Genomic_DNA.
DR RefSeq; WP_043873459.1; NZ_CCVW01000001.1.
DR AlphaFoldDB; A0A078KZ90; -.
DR STRING; 1034943.BN59_01322; -.
DR eggNOG; COG3850; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000044071; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:CDZ77043.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000044071};
KW Transferase {ECO:0000313|EMBL:CDZ77043.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..525
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 676..792
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 812..910
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 724
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 851
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 912 AA; 102728 MW; F3574D4ED1C332A1 CRC64;
MKKLGIKYQL RITSLIPVFV VALLFAVFYN GQFNKDLNQH MSRLGEAYIR QLLPAVQFAM
MRNDSRTLQS LINASTINPE VQALAFYNAQ GQLLAYRGGK HSIHKPFKPP EFTGDYIESK
QIKPYTINFL APITIPKFNL YSTTPFKTTS SNPIALEADD ILGWLSIDID TQSILIKRYR
MYIITIFITL LGLLISLTIH YFISRRIYIP ISRLRRSMKQ ILSNEFETHI PVSSSGELGL
IERGCAHLQK QYLNTIHDLN HHIEVATGDL QQSLELLEEK NIELLLEKKK TEEKSRQKSE
FIANMSHEIR TPMNGVIGFT NVLLESKLDS LQLDYVKTIK SSAQDLLVII NDILDYSKMD
AGKLNLDCIP LDIRACIDEV LALASPNSHK KGVDLIPITE VNVPKTVLGD PLRIKQIITN
LVSNAVKFTD HGYVLIRTCI EQETEKDYTL CISVTDTGIG ISNEDQTKLF NAFNQADTTI
TRRFGGSGLG LVICKKLVEA MSGRISLSSE VNKGSTFSAR IKLEKLAAYE IEKNQSQRFD
NIKVLCFDDN PLYLEAMCNG LAYWGIESVP VKALNKLEAA FTKHSECTLA FINVNEGCEK
QVAQILRKQS KACILVSKWM IHDPQSLGGC AFLFKPISIQ KLHETIELLV NQVTQSLTSN
HELDNLRSQL RLAHPELLIA EDNPVNRMLL NSLLSEHTNI EAVDNGEEAV QACQSKRFNV
ILLDLQMPKL NGLDAARMIR QESMLNKQTP IVVISANSSD LNNERLQKAG VDLCLQKPID
EKQLLNQILL FLKKSKPSAI DWQLCVQKVS GNQALAEEFL ARFVEELHKN RVEFLQLLQN
KDIKGLEAAA HKLHGACCFC GVPHLQTQVI RLEKQAKHAK GVEELKTSFA ELIQSIDEVI
DEFNNLYQTS AS
//
