ID F7NSJ6_9GAMM Unreviewed; 1850 AA.
AC F7NSJ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Rhein_0729 {ECO:0000313|EMBL:EGM79111.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79111.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM79111.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM79111.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(2011).
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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EGM79111.1}.
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DR EMBL; AFHI01000005; EGM79111.1; -; Genomic_DNA.
DR RefSeq; WP_008897622.1; NZ_AFHI01000005.1.
DR STRING; 506534.Rhein_0729; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000004282; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; 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 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1016..1064
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1132..1354
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1372..1492
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1520..1636
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1675..1774
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1425
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1569
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1714
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1850 AA; 204832 MW; 22F5DD40BD20583F CRC64;
MNPLYLLGIR LLASVIPALL MFTVAATQQK IEKLSVYSRL ANPQIYSVAN DHQGFLWFGT
TDGLKRYDGY QFVSFQHEPD QPGSLSNNNV GVMLHDSQSR LWVGTWGGGL NLYQPQSQTF
RHFRHDPELP GSLGADRVQS LFESKSGDIW VGTNGGGLNL YQPQSGAFKS YTHDPANPQS
IGNNRIWGLA EDSKQNLWVA TTDGLYRFDA KQQQFHKYGV AEGSLDHPEV RSIFIDAQDQ
LWVSTRLSFG RFEPDNNSYQ RYALPDGELP SVNSMTAQGD LLILATLAGV YHFNTKEKSF
RPAALNGDWS LLGSHDVRQV LLDSTGLLWA ATRYAGVVKV FPRLPAFEGW NNYLSHRPLS
GLYSQVQSMI AKPDGGLWLG TGKGLVAFDG QQQFSPLTSA SFPGQFTRFR IKTMAYDSQD
QLYINTDSGL YKLEPHQLQI HQLSMDWLKL AGDGVESLAV DKDDQLWLVL SSTHHLVRWD
PKTNTTDYFL KDVDPVFSFV DQQNEIWVAT LGDGTYRISA DRTQISHFLP ATSQSLSNTN
LSTASVLAIV QADADSLWFA TSQGVDLYSK KTGTVTHFKH VIEGEVISVQ SMALDTNGML
WLATSHGVSR LDPDTGIFNY FTTNDGLSSN GFLPRSVTQT PDGRIFFGSV EGITAVYPSQ
VRVNEVPPPV VITSVRIDGK QQSFPLPELL EVAADFKNLS IDFTALDFQA TEDNRYQTRL
VGYDDQWSNR TPEHKVNYGR LPPGDYQFEV LGSNNHGVWN PNPQRMKLKI LPPWYQTTVF
LVTAPLTLAL LIFFWFRART RAQREREQHL TEQVSRRTKD ILLLGELGKD IAATFELEQV
AQKIYNHLTT VLNTDTVALG LYDQQRSEVN YLFAMRKGER VDPVSVQLNN PRRPSCYCIE
QRQEFILSTP SDWARYGLSP QHCLNGPQTQ TVICEPLIAG EQLLGILSIQ SDQNDAFSEA
KINMLRIIAS HAAVSVSNAL SFQQLSETRQ RFEMAMIGAN AGSWELNNQT GELITNEIWA
TMLGYTPDEL LASYGNTIDQ LSQLVHPDDL ARTQAAFVHH IKGFSDVYRV QMRMKSRSGQ
WKWMLSVGKA IQHKVFGILL DVSESKAMES ALLEAKEKAE QATKAKSDFL SNMSHEIRTP
MNAIIGMSHL ALDTELAPKQ RNYIEKVHRS AEVLLGIIND ILDFSKIEAG KLDIEQTEFQ
LDTVLEQLVD MVGLKAAEKH IELHFSIAPD VPTVLSGDPL RLGQILTNLG NNAVKFTEQA
GEITVSVHCE QQEANQVLLH FAVKDSGIGM TAEQQAKLFQ SFSQADSSTT RKYGGTGLGL
AICKTLTELM QGEIWVESSE GQGSTFHFTA RLGVVTQPQT ATGLPDSMTG LKVVVADDND
TARDILAGLL RHQGFDVTST DSGEQALSVV READQQQPFQ LLCIDWNMPG LDGLATIAKL
QQLPLLSPPK IMLVTAYGTD EARQAAVHLK IDSYLAKPFS RHSLLQAVLH SFGHNSQVSS
KETGITAKVQ AAIRQLRGAR ILLAEDNILN QELAMELLSS NGLVVTLAEN GQQALDLLQQ
QHFDAVLMDC QMPVMDGYAA TAAIRQLGQF SQLPIIAMTA NVMAADIEKA LDAGMNAHIA
KPINVNEMFL VMAKWIKVAD PQPEVMPVSE DADQLQLPEL AGIDTEAGLA VSQHKQALYL
KLLKRFADSN QDFSQQFQQA LQDTDPEAAS RCAHSLRGSA GNIGAKAVQF AAQALEMACR
EHTDITAPLL QLEQELAVVL TSLQQLSQSQ VSAEIQEADP QQIQSLLEEL TALIADNDTE
AVDKAEQLQL LLSGTEYKVA VAALLKHINN YDFDEAAASL TLLSQQIESQ
//
