ID A0A1R1CAF6_9BACL Unreviewed; 538 AA.
AC A0A1R1CAF6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BK127_07790 {ECO:0000313|EMBL:OMF19040.1};
OS Paenibacillus sp. FSL H7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF19040.1, ECO:0000313|Proteomes:UP000187480};
RN [1] {ECO:0000313|EMBL:OMF19040.1, ECO:0000313|Proteomes:UP000187480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF19040.1,
RC ECO:0000313|Proteomes:UP000187480};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OMF19040.1}.
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DR EMBL; MRTH01000004; OMF19040.1; -; Genomic_DNA.
DR RefSeq; WP_076229453.1; NZ_MRTH01000004.1.
DR AlphaFoldDB; A0A1R1CAF6; -.
DR STRING; 1920421.BK127_07790; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000187480; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OMF19040.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000187480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..528
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 538 AA; 59525 MW; AB8A8C5081F0B948 CRC64;
MLQRLKINWK IAFLSFGIVV FSLLIGGTIL VGSIISLKED ELGRRLLVTA RTVAQMPEVA
GSLSTPQQKD TSMQAAAERI RIINDVTYIV VMDMNRMRLT HPVESNIGTY SRGTDEGPAF
AEHTYIARAK GELGTALRAF VPVMNADEHT QVGVVLVGQL LPSVGQVLLE LSGQAYLILL
ISLVFGIWGS WLLAQHIKKQ MFELEPHEIA QLLTERTATF HAMHEGVIAI DKHERITICN
DPAKQMLNIQ GEVIGRMIRE VVPDTRLPEI LVLNQPIYNK ELQIGHAVIM SNRVPITVKG
QTVGAVAIFR DRTEVAQMAE ELTGVRTFVD ALRVQNHEYM NKLHTIGGLI QLGSTDRALD
YIFEITEQQV ELTQYLTQRI KNDSLTGLLL GKISRGKELG ITLEIDRQSH LEHLPERIDD
HDFVILIGNL VENAFDALGG IRADKRIFLS IEQDEEVLSI LVEDNGCGID SAIQEKIFEQ
GFTTKGSGGR GIGLYLIASI VRKGDGSIVV DSKPAEGTSI FISFPMRLSQ ETTVPGVN
//