ID Q7UUC5_RHOBA Unreviewed; 1998 AA. AC Q7UUC5; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 147. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=RB3373 {ECO:0000313|EMBL:CAD73156.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD73156.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD73156.1, ECO:0000313|Proteomes:UP000001025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10527 / NCIMB 13988 / SH1 RC {ECO:0000313|Proteomes:UP000001025}; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., RA Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX294138; CAD73156.1; -; Genomic_DNA. DR RefSeq; NP_865472.1; NC_005027.1. DR RefSeq; WP_011119328.1; NC_005027.1. DR STRING; 243090.RB3373; -. DR EnsemblBacteria; CAD73156; CAD73156; RB3373. DR KEGG; rba:RB3373; -. DR PATRIC; fig|243090.15.peg.1557; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0642; Bacteria. DR eggNOG; COG0784; Bacteria. DR eggNOG; COG2198; Bacteria. DR eggNOG; COG2203; Bacteria. DR eggNOG; COG3899; Bacteria. DR HOGENOM; CLU_000445_34_2_0; -. DR InParanoid; Q7UUC5; -. DR OrthoDB; 9762493at2; -. DR Proteomes; UP000001025; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 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; -; 1. 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR041664; AAA_16. DR InterPro; IPR011006; CheY-like_superfamily. 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; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000719; Prot_kinase_dom. 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; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1. DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1. DR Pfam; PF13191; AAA_16; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF01627; Hpt; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF52172; CheY-like; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50894; HPT; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAD73156.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Receptor {ECO:0000313|EMBL:CAD73156.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001025}; KW Transferase {ECO:0000313|EMBL:CAD73156.1}. FT DOMAIN 17..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1438..1661 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 1694..1810 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 1888..1978 FT /note="HPt" FT /evidence="ECO:0000259|PROSITE:PS50894" FT REGION 1839..1858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1975..1998 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1401..1431 FT /evidence="ECO:0000256|SAM:Coils" FT MOD_RES 1745 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" FT MOD_RES 1927 FT /note="Phosphohistidine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110" SQ SEQUENCE 1998 AA; 223221 MW; 519D77C28A32742C CRC64; MSSLPPNDPD AISTQRYNVQ KKLSNASVVS CFSAIDTATG GKVILREVPK VFFQERGFHR FKTESRLTSG IHCETYSRPI DFMVGETHLR VVYPYVEGVS LARKFRKRPL TATEAMLLAK DLFEALEQIH QIGCIHRDIR PSNIIVREDA RSVLCGYVPL WCPELFGKDD LLARECATYT SPELSGIIDH DISETSDLYS VGHVLYAALT GVPAFAGDVS EILYRHMTAD PDTGCYPDET PSVVIALVEK LIRKEPRDRY QSASAVLDDV KTILHQLKTG GVADDFVIGN TDKRTVVIDP AFVGRDEHVR TLEKSLDNVL EGRTERVLLR SESGMGKTRL LNEVSRLASR KRFLVLRGRS LPDANQQPSA IWLQAMDQLV KHLTNDPVML ERTRERMEPY RQEVTTALPA LAKAFGWGNA KLSGPDEFGQ GRIVSAFRTL FTELGTPETS VMITLDDCQW MDDQSFRILQ AICECPARHL FLFAVTRPSE GLCTRLNDEL SFPIKLELGP LTDQAVQQLA ESMAGQLPTE AIEVVQRFAG GSPFMASAIV RGLVESSALR PADKCWVVDD AKLSSFQAAD DASEILVDRL TRLPVETREL LTAAAVIGRD FNLEVAAELV GIRLADAHRA IHPARVQRLV WSRPDRVLAF VHDKIRESIL EELTADRIRS MHGQIGQYYV EHEPLEFFKL AYHFDAAELH EQALPFALRA AEIARNSFSL VSAEEQLRIA TRAICHADRS KQHHIQMMMS DVLMLQGEYD KSEAWLDQAF ESAETGTHNA RVLLKRGELH FKRGSKNLAV ECFEASLRQL KQPVCNNRLS LMARIALEGA RQVRNSLLPC FVGRQCGQPS EEEQMSLSLY SQIAHAYWYT RDKYYTLWAH LRSMNAAERF QPTRYLAQSY SEHAPVMTLL RWEKRGVEYA RRSLEIRKAF SDVWGQGQTR NFLSILLLSF SRYEQCVEQA SQAVKMLERT GDYWEVHIAR YQLAASLYRL GRHKEALEQS RINFESAMRR GDYQATGNII DVWARSTNGD IPEEIIENEL ARDLADSQRM SQVLLAKGVR EFYQERFAEA VGSFSRAIAV AEDTRVSNTY VSPAYPWRCT AMRRQLETSI PRSTQRRWKS IGELGRATRK AVAVSKQFTN EIPHAYRERG AYLALAGKLR ASQACFQKSL QVAEAQGAMV AHAKTMILFA EYAAEFGWPI DGDAIEHARG TLSELECSDY DVNEGGSLSL VNRFDSLLAS GRRIATSVLP EQIYQEVRRA ATKILRGEQV FLITRTEDER LSTVPAGMPF DPAIVNEVDR TRQTVVADVE NAVSNGITTT KQGTFLCSPV DVNDQTLSYL YVSNERFSNL YDDDEIRIAD YLTSAAGAAM EKANSFQQLQ DLNLNLEKKV HERTESVVRH SKELELTAQQ LTATKEKLQI AKTAAEEANQ AKSEFLARMS HEIRTPITGI LGFTELLLRG VVTDDAERES HLQTIHSNGF HLLHLLNDIL DISKIEADKI ETERVLCNPS WMVQDVIASL RSKAIEKDIS LEIQVDSEFP EEIYSDPTRL RQILTNLTSN AIKFTNQGGV TISISAIGSG ETASKMKIAV RDSGIGMTQE QTAFIFEPFK QADVSTTREY GGTGLGLSIS KRLAEALDGT LEVESERGVG TQMILNFDIE CPSGVRMLSP AEVLLPYNGV KENQFDVVDL AGVRVLVVDD CETNRRLLSL LLQDAGAEVD IRCNGREAVD ALRSDPSMVD IVLMDMQMPV MDGYTATSAL RAQGFQAPIV ALTANAMTGD EVRCREAGCT DYQTKPLDLN ALLQCVAENT VGEKANVSSI VAVQENPPVI EEAASPIELS SQSVGQGEPL AESSEMLPDD HEQLEVALNE EHEPLNDEDE TTKEKIFNYD WLHEFACDLI DQLDETMPSI INAYDRGDLE QVGKHLHQIR GSGGTVGLLQ LSEIAAKGES AIEVSQWEQL RNTLTELQSY VSDALEEKSS SSESVSNNSL DPSADIDR //