ID A1US03_BARBK Unreviewed; 773 AA.
AC A1US03;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BARBAKC583_0438 {ECO:0000313|EMBL:ABM44919.1};
OS Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM44919.1, ECO:0000313|Proteomes:UP000000643};
RN [1] {ECO:0000313|EMBL:ABM44919.1, ECO:0000313|Proteomes:UP000000643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583
RC {ECO:0000313|Proteomes:UP000000643};
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000524; ABM44919.1; -; Genomic_DNA.
DR RefSeq; WP_005766478.1; NC_008783.1.
DR AlphaFoldDB; A1US03; -.
DR STRING; 360095.BARBAKC583_0438; -.
DR GeneID; 72471951; -.
DR KEGG; bbk:BARBAKC583_0438; -.
DR PATRIC; fig|360095.6.peg.420; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_71_5; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000000643; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12860; PAS_7; 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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000643};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 553..772
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..553
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 773 AA; 87605 MW; EA8E58E53FD2B5C1 CRC64;
MAKLDVYNAP TETHSDAKSS AQSCKTRTAH INHLSDSNYK RLLFIEPWLR RFIPFIIITF
LIVLAAIRFV LIYDWHNAID KDTRSKITLL TTHIINIINR DLLSATKKER KAILSHNHLQ
NILINFQNEG LTNTNTMITI IDQNRNVLAS SNPDITLGKP LQDFIPQSTA LWTLGKYTGA
MQIMIGEEPA LASFHETENG QYGVFISEKT HHIYMEWHKV FSLNLILFIG TASIILALLY
AYYTQVTRAR NTDLISEKIQ NRIDMAMMRG RCGLWDWNMA SGRIYWSRAM YEMLGYVPQD
ALLSISQITA IINSTDINFF DLAQELMSGE KKHIDINVPM RHADGHHVWM RIRAEVTEEE
EPHLVGISFD ISEQHQFVEQ TAQADLRIRD AIENISESFV LWDSEGRLVM SNSKFCEYAA
IPKQMLQSGI QRATVTAMAR PAISEYFLKE DDGTGNLTSI RQTADGFWLK INERRTQDGG
LVCIGTDISE LKQQQEKFED SERRLFSFIQ ELKRARGNAQ QRATEVEKLN KSLQAEKERA
ESANKAKSEF LANISHELRT PLNAILGFSD IMLQSTFGPL GSQRYEEYMR DIHNSGTHLL
TLINDILDMS KIEAGRFTLD CKNVDLEPII SEAIRTLTPQ AQEKKISITA NIAPKLHAEL
DCRAMRQIFL NLISNAVKFT PSGGSIDICA FQKKNNLIFK IKDTGVGIPQ SAIKKLGKPF
EQVENQFTKT HTGSGLGLAI SRSLLELHKG KLEIASEEEN GTTVTITIPI KQN
//
