ID K1Y2A3_9BACT Unreviewed; 641 AA.
AC K1Y2A3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=ACD_75C01282G0001 {ECO:0000313|EMBL:EKD37040.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD37040.1};
RN [1] {ECO:0000313|EMBL:EKD37040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(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};
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:EKD37040.1}.
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DR EMBL; AMFJ01031951; EKD37040.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Y2A3; -.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EKD37040.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EKD37040.1}.
FT DOMAIN 54..103
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 132..182
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 183..227
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 255..307
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 325..547
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 572..641
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 6..33
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 621
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 641
FT /evidence="ECO:0000313|EMBL:EKD37040.1"
SQ SEQUENCE 641 AA; 71643 MW; 492E59DB609E6B0F CRC64;
MSMTTTTELQ QELQQAQQRI AELEELVARQ TGSVLITSYD LSLCGQQKDE LTQSRNKYRK
LFNYANDAMF VISLDRNSSN YGFFSDVNNV ACKRLGYTRE ELLQLTPFDI SDGKNIEYNQ
ELVARLSKEG NATFETTYVK KNGTLLPVEI SALRLTIDGK ELYMAIARDI TERKQAEEAL
RTSENLYRLL ADNVHDVIWT TDADLKPRYV SPSFSHLTGF AREEALSTIY AKIIVPSPFL
ANHAQLPSLA EQLPLHWESE VLTAGGETIW VESIASLLPE SSRRCTGIIG VTRDITSRKR
IMNELQAAKE QAFAANKAKS EFLANMSHEV RTPMNGVLGM LQLLEMTELD DEQHEYIDTA
MESGKSLLTI INDILDYAKI EAGKLPLTPE EFQIREVIRT LINSFRTAVN PHKVKLIAEV
SPDVPEFLVA DHIRIRQILY NIVGNAVKFT ERGEIRISLD MAELPVENKV QLTCSIADTG
IGVPDNIGDK LFEPFTQIES PRQKKIKGTG LGLSIVKQLV LLMNGTVNLQ RNSAGGTTVT
FTLLVDRGSG QSVKNSLAAP TPILTSPSRR LSALIVEDEQ INQQILQAIL LKLGHRPTVA
ENGYAALDLL ESRHFDIVLM DVQMPELDGL ETTRIIRNSH D
//
