ID G2PXA2_9FIRM Unreviewed; 612 AA.
AC G2PXA2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Calla_1261 {ECO:0000313|EMBL:AEM73881.1};
OS Caldicellulosiruptor acetigenus 6A.
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM73881.1, ECO:0000313|Proteomes:UP000009257};
RN [1] {ECO:0000313|EMBL:AEM73881.1, ECO:0000313|Proteomes:UP000009257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6A {ECO:0000313|EMBL:AEM73881.1,
RC ECO:0000313|Proteomes:UP000009257};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Blumer-Schuette S.E.,
RA Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor lactoaceticus 6A.";
RL Submitted (AUG-2011) 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; CP003001; AEM73881.1; -; Genomic_DNA.
DR RefSeq; WP_014042592.1; NC_015949.1.
DR AlphaFoldDB; G2PXA2; -.
DR KEGG; clc:Calla_1261; -.
DR HOGENOM; CLU_020473_6_0_9; -.
DR Proteomes; UP000009257; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; 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 InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEM73881.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..384
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 502..605
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 384..411
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 612 AA; 71641 MW; D7E00BB43BCC188A CRC64;
MWWNKVLKKF FKFSKERLLD KLDNLSVRKK LLLVYILCVL IPTIVSHFIF TICIVKNLQQ
QKINQIKSAF NILNTNVKRV IDEAILYSNT LYTDDLLNDM LDIDYHGMDD FYSNYVQYLR
NRIYQGRNVY SDIARVTIYT NNPTILNSDG YRKLNIQEVK EWYDKVINNP QGIVVIPTSD
SGVNGEEGYV SLLRNLNQYE QRSTSTGNNS KYTKIAKIDI YLSSFFNSIN FEVFGGEIYL
LDSSNRIIAA HTYNNLIFTK PFVKFETSKF VPKGSYVFVN NLDITLLSGW KLVGVFSRSY
MMGEIYRAIE FILLISLLSL IFATFLIRVI TTSLSNRLEL LERHIRKVKK QRFEILTCRE
GNDEIGSLIR EFNNMTVRLK ELIEKEMLSE IQKKTLEVEK KQAEINALQS QINPHFLFNT
LDSIRMRSVL KNELETAEII KYLTRTLRRL IYWGNDITTV QEEINFVEDF LKIQQYRFGE
KLTYEIFVEE DAKNCLIPKM TIQPLVENAC IHGIEEKEDS GRVTVRVKKE GVKLMIEVSD
NGIGMDEKKL EELYSNLNNP LYDKSIGLKN VYRRLMLYYN DNAEFYIESS FHKGTKVIIK
LPLELPVFVH KI
//
