ID A0A0C2G247_9ACTN Unreviewed; 1126 AA.
AC A0A0C2G247;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LP52_19270 {ECO:0000313|EMBL:KIH97398.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97398.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIH97398.1}.
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DR EMBL; JROO01000038; KIH97398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2G247; -.
DR STRING; 183763.LP52_19270; -.
DR OrthoDB; 3845898at2; -.
DR Proteomes; UP000031675; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR013587; Nitrate/nitrite_sensing.
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 Pfam; PF08376; NIT; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675};
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 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..446
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..141
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 759..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 121913 MW; 867E37FCF33BF464 CRC64;
MSTRATDDGG GAARGEPQAD RAAAPAEGRR RWLAPREWRV RPRLIALIVI PTAVALVLGG
LRISESAVNT VTHDRIEEAA ALGEAVVDLS TELGRERLQA SAYIADDPNY DERSEESLAA
LQDQIKESRQ AEQRVQSLID SLGDPGTQLM ATRLQSMQAS LGNLDRVRDE VQGTRLTVLP
MVTKYTQVLD SLADFNQTIA ESTSDTELRE SVRALTGVAN ARAELSYEGA LMVHSLLRGS
MSEGIRSEIE DSRATFENER DNFRNSATTD QRQMYEETFV GAEVSQMSTT RLRIVMRARD
GQDLSGLTPG DTPAEYQEVV GSVLDKVNEI ESNLATSVRS QAASLRTDAL NRAIVESVLV
LAVLISVFTL TSLVVRSLVR PLRALREGAL RIAEEDLPGA ISRMQESSAA AGEVEVSPIE
VRSRDEIGEV ARSFDEVHRV ALHLASDEAA LRSNVNAMFV NLSRRSQTLV ERQLRLIDGL
EQGEQDDERL GDLFQLDHLA TRMRRNNENL LVLSGQDNTR KWAQPVPLVD VLRGAVSEVE
EYERINVRAP SHISVLGRPV NDVIHLVAEL VENATSFSSH DSPVAVTAQV MEDGGVRVEV
TDSGIGMPPE EIRAVNERLA EPPVIDVGVS RRMGLFVVSR LAARHGIRVQ LDEAHNGGIT
ASAVLPPDLL ITPVEPQAAL DASGAPGTPD TYAEAAAAFA ANPAPPEPSI WGERRDAGEP
QLPKREPGIN RAAGFASDEH PPSGEDLWQG SGWNLPPEQP EQSRPPQPEQ SRPPQPPAEP
PQPVEPPRAE PPRPVEPPRA EPPRQPAEPQ AGAPQWDAWD SRRWREQRPG QQHHEEAPTQ
SFAQAAEAAN PWASQSGPAE NGWANGANGQ PQQVGRPEDA RQQPARTEAG RQEWNEPENR
EGSGSAAYLS RRYGGGAGQD TVVPPSPESG SETLPIFDAI ESNWFRRRSG GPATEPETGP
LPRFGADSAA GAEYDRGRSE QPYQGSPAAQ APRYGAETAG ANGSSGQQGD QHMQQDQGAP
GARQPYDSPA SAAPQPYGTE DDWRSEADRG WEAARTAAEP MAGGLTTSGL PKRVPKANLV
PGTAPEPDNV KQVPPRSADR VRNRFSGFQR GVREGRSQIG GNDEEN
//
