ID A1T4V4_MYCVP Unreviewed; 482 AA.
AC A1T4V4;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mvan_1370 {ECO:0000313|EMBL:ABM12204.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM12204.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM12204.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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};
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DR EMBL; CP000511; ABM12204.1; -; Genomic_DNA.
DR RefSeq; WP_011778633.1; NZ_JACKSD010000069.1.
DR AlphaFoldDB; A1T4V4; -.
DR STRING; 350058.Mvan_1370; -.
DR KEGG; mva:Mvan_1370; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_81_11; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF48; TWO-COMPONENT SENSOR HISTIDINE KINASE-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 46..125
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 300..477
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 482 AA; 52730 MW; 953A681F87C24A61 CRC64;
MTEQGERSAC VIDELRGLFL FDGLTDAQLT ALCADGWVQT FPAGQLCREG DPARYFYVLL
DGEIALSKRS GDRDVDIWRA AEPGVYCGAW SAFLRDPDLT YENSATVTRP SRLLVLDAMT
LGDFLVTEFP MASHLLVGHS HGRFHAHRIL GPHDRLVALG QLTAGLTHEL NNPAAAAVRA
AHGLRTQIAA MRHRRAELPE NALPPEAMSS LVELQDRVAE AAGKPKDLTS VEKSDLEEAL
GRWLEARGVD DAWEHAATFA EAGLDIDWME RISASRCCDG PTSLSAVIRW LAGTAETELL
LTEITDATKR ISTLVDQAKR YSQLDRAPFD VADVHELLDS TLTMFSHRLG DAVTVVRDYD
LGLPDLPCYA AELNQVWTHL IANALDALAG QPAGVLTIRT RHEQHMARVE VCDTGGGIPD
DLLTRVFDPF FTTKPFGEGT GLGLDIAARI VDRHRGSLWA ESTPGDTRFI TSLPLTVEPA
RP
//
