ID A0A168MRG2_9BACL Unreviewed; 1819 AA.
AC A0A168MRG2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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};
GN ORFNames=PBAT_13525 {ECO:0000313|EMBL:OAB44969.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB44969.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB44969.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB44969.1,
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:OAB44969.1}.
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DR EMBL; LVJI01000018; OAB44969.1; -; Genomic_DNA.
DR RefSeq; WP_068650440.1; NZ_LVJI01000018.1.
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; 8.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 6.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 6.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 9.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
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 SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR PROSITE; PS50885; HAMP; 9.
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, ECO:0000313|EMBL:OAB44969.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 103..160
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 200..252
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 292..344
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 384..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 476..528
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 568..620
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 660..712
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 752..804
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 844..896
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1141..1374
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1422..1535
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1544..1661
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1690..1807
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1065..1131
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1471
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1593
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1740
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1819 AA; 201206 MW; 14D2C249A473335B CRC64;
MSNKDSFDEQ TNEQFNTSEL LQALNAFKQG DFSYRIPVDL VGVEGKVAES FNEIMEMQEN
MVIEIQAVAK VVGKEGNLSR RFSHNNTGES WTVAVEALNG MVTDLIQPTS EMVRVINAVA
EGDLSQTVEL EFEGRPLTGE FRKSANNINM MVNQLSKFAS EVTRVAREVG TEGNLGGQAD
VEGVSGTWKN LTDSVNNMAT NLTDQVRNIA VVTTAVANGD LSKKITADVQ GEILELKITI
NTMVDQLSMF ASEVTRMARD VGTEGILGGQ AEVSGVAGTW RDLTESVNYM ASNLTNQVRN
IAEVTTAVAK GDLSKTITVD AKGEILELKS TINTMVNQLS NFASEVTRVA REVSTEGKLG
GHADVKDVSG TWKDLTDNVN FMAGTLTDQV RNIAEVTTAV AKGDLSKQIT VNAKGEILEL
KNTINTMVDQ LSTFASEVTR VAREVGTLGM LGGQAKVKGV AGTWRDLTES VNYMASNLTD
QVRNIAVVTT AVANGDLSKK ITADVQGEIL ELKNTINTMV DQLSTFASEV TRVSQEVGTE
GKLGGQAQVK GVGGTWKDLT EGVNSMARNL TDQVRNIAEV TTSVAKGDLS KKITVDVKGE
MLELKNTMNT MLDQLSNFAS EVTRVAREVG TEGKLGAQAE VKDVSGTWKD LTDTVNYMAS
NLTIQMRNIA GVTTAVANGD LSKKITVDVK GELLELKNTI NTMVDQLNSF ASEVTRVARE
VGTDGKLGGQ SQVRGVGGIW KDLTDNVNIM ATNLTDQVRG IAKVVTAVAK GNLQQKLNVE
AKGEIAELTD TINNMIDTLA TFADQVTTVA REVGAEGKLG GQASVPGAAG TWRDLTDNVN
YMASTLTTQV RAITNVATAV TKGDLSRTID VAAAGEVAAL KDNVNEMIRN LKETTRINTD
QDWLKTNLAK FSRLLQGQRD LYAVCRMILS ELAPLVSMQH GVIYINEVVS DEPVLSLFAS
YAYQQRKHLS NSFRAGEGLV GQCLIEKQRI LLTNVPSDYV MISSGLGEAT PLNIVLLPII
FEDQVLAVLE LASFRAFGEI DLAFLDQLTE SIGIVINTMQ ANQRTEELLI QSQSLTEKLQ
KQQMELQNTN EELEDKAKLL VIQKAEVESK NNEVEIAKSF LEEKAEQLAL TSRYKSEFLA
NMSHELRTPL NSLLLLAEQL AENPEANLSN NQVKFAKTIQ DSGFDLLNLI NDILDLSKIE
SGTISPDYTE IKLLDLVDAL DRTFRHMVDD SKLEFKIKTD NNVPTTLVTD SKRLQQVLKN
LLSNAFKFTD VGQVMLHIRR ATDGWNLANT ILNNASMVLC FSVSDTGVGI PEDKQRIIFE
AFQQADGSTN RVYGGTGLGL AISREIAAML GGEITLYSVV DKGSFFNLFL PMDTEYQEIE
VETKYVPEVI DVTPPERKYS DSRKRDNDFV DDRDLIEPGD RVFLIIEDDL KFNEILLDLL
HKRNIKAIIT TKGSNALELA RKYKPVAITL DLRLKDTDGW LVIEHLKNDL NVRHIPVCVI
SVEEDEIQLM QKGVYDYICK PINNEELENT LDNLNRYADQ MNHNLLIVNS DTETSQQWKE
VIDNKDVQMT DIDTARKALD YLKINDVDCL LVDNDLKDMD VLQFIREIQK NPKNKYLRMV
LYRTKKWTHE EEHELEELKK VAVIREVKSP IQMMDETSVF LHRKSENLSE GSREAMIKLH
QSDEMIKYKK VLVVDDDIRN IFALTTILER HNMMVISAEN GYEAITLIEQ SSNIDIILMD
IMMPIMDGYE TIRAIREKPE FQKLPIIALT AKAMAGDREE CLEAGASDYI TKPVNSAHLL
SMIRSWLDTA VEEEPIEID
//
