ID   H6R0M8_NOCCG            Unreviewed;       929 AA.
AC   H6R0M8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=NOCYR_4743 {ECO:0000313|EMBL:CCF65497.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF65497.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF65497.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF65497.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA   Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
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; FO082843; CCF65497.1; -; Genomic_DNA.
DR   RefSeq; WP_014352948.1; NC_016887.1.
DR   AlphaFoldDB; H6R0M8; -.
DR   STRING; 1127134.NOCYR_4743; -.
DR   KEGG; ncy:NOCYR_4743; -.
DR   eggNOG; COG0642; Bacteria.
DR   HOGENOM; CLU_002554_1_0_11; -.
DR   OrthoDB; 4652229at2; -.
DR   Proteomes; UP000008190; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCF65497.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008190};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          319..386
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          503..613
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          616..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..660
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   929 AA;  98971 MW;  FE879AA29D5748F6 CRC64;
     MEAAPRPWQF SLPNWSVTRK VGIVLVLPVV LATVFAVLRI NNELQTMDQL DAATEQAIII
     RPIVKFGTAT EHLAVTATSS WGNPADPRTD AALTRFDQAL ADMETALQDT GVSGKVTAEL
     SSAVAIGTTM RNSLRSGSPA MVGDQADEIG MRIGNALALS PSVEDLVIQR YFLQLTTIQT
     ARRVLTEQRM LISSPDAARN PSMRARVLTS AGAELTMIYQ YGQILPELAG NMRPLLDAVQ
     TRLATFSQNT ADPASNPAVL DSLQVSADTY DATTAQLTDI IDAALLERTT TAQNSALRET
     TIVIAVLLAG LALALAVART LVVPVRRLRR DALEVAHVKL PDELSVVRAG GTTPAITPVA
     VHTTDEIGQL ARAVDEMHEQ ALNLAAEQAR LRVQIGNMFE TLSRRSQSLV EQQLALIEDL
     EHDEDNSERL QSLFRLDHLA TRMRRNGDNL LVLAGTALRR GQLQPVPLSD MLWSAVSQVE
     DYQRVEIGTV PDGVVAGEPA VDIEHLLAEL IDNALRYSPP TTPVAVTVSR AVDGGYLIEI
     TDRGLGMSAE DLQATNERLA SGGEVTVETA RRMGLFVVGR LAKRHNITVS LRRTSTMAQQ
     PGITASVHLP GALVAPAMDD ADGKPQTDPF AALPPGAPPQ RTLVPVPSLP EAPAPAPESE
     PVPLSSWGTT SSGLPQRRPS IRVAEPPEQP TVSVPASARP DSGAEDRSTN TPFGPPTPEP
     HPGDAETGPN RIVSAEPEEE PTGLWAETKE HPIVAPQPEP EPRATTAGSG LPIRRPAPVR
     DEPQQQAPEP PRPQEPETVT VTAESAAATS TSTRLHPVGG DSPTPIYQRM VSEWLVEPAT
     AQPSSGTWSS PADAGWMAAE DAAKPTTSAR TVGGLPIRRP GAQLVPGGLA PVEEAGARDP
     EEIRNNLTRH LSGVRSGRAE AQHNDGGLA
//