ID Q73UP5_MYCPA Unreviewed; 499 AA.
AC Q73UP5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MAP_3321c {ECO:0000313|EMBL:AAS05871.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS05871.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS05871.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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; AE016958; AAS05871.1; -; Genomic_DNA.
DR RefSeq; WP_003874605.1; NZ_CP106873.1.
DR AlphaFoldDB; Q73UP5; -.
DR STRING; 262316.MAP_3321c; -.
DR KEGG; mpa:MAP_3321c; -.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_045351_1_0_11; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR Gene3D; 3.30.450.280; GAF domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR038424; H_kinase_PdtaS_GAF_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR022066; PdtaS_GAF.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF12282; PdtaS_GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 298..493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 499 AA; 53743 MW; E7496B1968A28D08 CRC64;
MSTLGDLLAE HTMLPGNAVD HLHAVVGEWQ LLADLSFADY LMWVCRDDGM LVCVAQCRPN
TAPTVLQTDA VGTVVASERL TLVAETFASG AAKADDVAAQ QDSWLPGTHV EASPVRYGGH
VVAVLTRHQT AVAADRASGQ LEIAYRECAA DLVHMLAEGT FPDVGDVAMS RSTPRAGDGF
IRLDVNGVVA YASPNALSAY HRMGLTTELE GHNLIEITRP LISDSFEAQE MAEHVKDLLA
GGKSMRMEVD AGGATVLLRT LPLVVNGASA GAAVLIRDVT EVKRRDRALI SKDATIREIH
HRVKNNLQTV AALLRLQARR TTNPEGREAL IESVRRVSSI ALVHDALSMS VDEQVNLDEV
IDRILPIMND VASVDRPIRI NRVGDLGVLD SDRATALIMV ITELVQNAIE HAFDPTAAEG
SVTIRAERSA RWLDVVVHDD GRGLPEGFSL EASDSLGLQI VRTLVSAELD GTLGMSEASE
RGTDVVLRVP IGRRTRMLL
//
