ID A0A168Q5I1_9BACL Unreviewed; 1217 AA.
AC A0A168Q5I1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PBAT_06830 {ECO:0000313|EMBL:OAB47407.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB47407.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB47407.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB47407.1,
RC ECO:0000313|Proteomes:UP000077355};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL Submitted (MAR-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:OAB47407.1}.
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DR EMBL; LVJI01000007; OAB47407.1; -; Genomic_DNA.
DR RefSeq; WP_068647848.1; NZ_LVJI01000007.1.
DR AlphaFoldDB; A0A168Q5I1; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000077355; 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 CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077355};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..267
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 543..772
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 830..943
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 952..1068
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1098..1215
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 425..526
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 879
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1001
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1148
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1217 AA; 137521 MW; CF2347C466DA0E3F CRC64;
MFKNSKFSIR SKIALGYLII LFCLGASIFV LNDQMSSMEK EITFITDHDM EVHNLAYLIE
KHVLDMETGQ RGFMLTGDEK YLEPYNSGIT KWDDDYNSLH QLITDNPSQQ KKLEGIKLNI
EQWIETVGEP TIAYKKENNM QDSLNFFKLD TGKLKVDRMR DQLDDFRTTE KSLTQIRVDD
LNQRNADLKF VLYVFLLTVT VISILVAFVI SRTIVNSIKQ VSTAISEIAS SEGNLTARRI
NIRTKDEIRD LGEATNHLLQ SNENEIWLQT SISEVATACQ GLASDSEIAQ SFISKIALLL
HASHGIYYRR TEGKLKMIAS FAAYGDNTAA SSFRIGEGLV GQCALDKRTF LLDPVPEDHV
KITTGLGQSS PRSILIVPIE YEGHVVGVIE LASLESFIPL QQQLVEKTRS TLGIAMNSAM
IQMEVQRLLE ESQALSEELQ SQTEELQQQT EELQAQSEEL TAQQDELKAS NDSLKFSEEQ
LQRQQEELEQ SNQEIAARAE QMEYLMRKTE ETNEQIENQN AILAKHATEL ISASQYKSEF
LANMSHELRT PLNSLLILSQ ILADNKEGNL HPKQIDFAHT IHASGSDLLR LIDEILDLSK
VEAGQMTVEL ETVFLEDVKE TMWRNFQPMA EQKGVEFQIH VEQSLPEAIH TDGHRLQQIL
KNLLSNAFKF TDQGQVMLRI YRMDLPEGSD PTDHSFLAFS VSDTGIGISK DKKDVIFEAF
QQADGTTSRK YGGTGLGLTI SRELSALLGG HIKIESHEGQ GSTFTLYLPE SQMSSQHFAL
KEVGAAGTDS TDVPLSIEML LPSIELSNPD LLLISEVEDD RNEVNAGDRV LLIIEDDIQF
AKIMLDMARS YNFKGIVALQ GDKGLALAHA YKPDAIMLDI QLPVIDGWAI LERLKQHPDT
RHIPIHILSV LDESKQGLMM GAMAYLQKPV NKDTIDNALS RIESFINRDL KRLLIVEDDV
VLRNSMVELI GHDDVVITAV STGKEALHEL QLEQFDCMVM DLGLSDISGF DLLDRIRHTE
QLQKLPIIIY TGKELDMKEE MQLKKYAESI IIKNVKSQER LFDETALFLH RVEANLPEDR
RKILKKLYNN ETAFDGKRIL LVEDDMRNIF ALSNVLATYN LDVTFAENGR EALELLEKDP
NFDLILMDIM MPEMDGYQAM KAIRAMPQFE KLPIIALTAK AMKEDRKRCI DAGASDYISK
PIDTVKLLSL LKVWLYT
//
