ID Q2SPR3_HAHCH Unreviewed; 560 AA. AC Q2SPR3; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 103. DE SubName: Full=Serine phosphatase RsbU, regulator of sigma subunit {ECO:0000313|EMBL:ABC27361.1}; GN OrderedLocusNames=HCH_00451 {ECO:0000313|EMBL:ABC27361.1}; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC27361.1, ECO:0000313|Proteomes:UP000000238}; RN [1] {ECO:0000313|EMBL:ABC27361.1, ECO:0000313|Proteomes:UP000000238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC27361.1, RC ECO:0000313|Proteomes:UP000000238}; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). 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; CP000155; ABC27361.1; -; Genomic_DNA. DR RefSeq; WP_011394438.1; NC_007645.1. DR AlphaFoldDB; Q2SPR3; -. DR STRING; 349521.HCH_00451; -. DR KEGG; hch:HCH_00451; -. DR eggNOG; COG2172; Bacteria. DR eggNOG; COG2208; Bacteria. DR eggNOG; COG3437; Bacteria. DR HOGENOM; CLU_000445_43_7_6; -. DR OrthoDB; 9811749at2; -. DR Proteomes; UP000000238; Chromosome. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR CDD; cd16936; HATPase_RsbW-like; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR PANTHER; PTHR43156:SF13; PROTEIN ICFG; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF07228; SpoIIE; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}; KW Reference proteome {ECO:0000313|Proteomes:UP000000238}. FT DOMAIN 2..117 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT REGION 377..402 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 383..397 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 51 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 560 AA; 62781 MW; 06113F6E9A15E79D CRC64; MNILVVDDDM YSRQLMGFVL EEGGHKCEFA ESGEQALEIW REQGADVVLM DVLMPGMNGY EAARIIKAEA GQDHIPIVFL TALDDDRALV ECLSIGDDFL GKPVNFVTLQ AKIRAHSRTL ALNRQVVEQN RELAYFHTKV QAEHEMTQHI MTAALKLSAK DVYGIRYHCT ARSTFNGDLV LLKEKRDGGA YVLVGDFTGH GLAASVGSIP VAQAFSTMCE RNLSVSEISL ELNKILRRFL PPTMFFAACL LEINSTRSKI ELWAGGLPDA FIVSGDNKIR RVIHSAHMPL GIMEMEEFES WTETISVTAE DRLYIYTDGI TECPNIANEM FGEERLRQVL ESGENNLFDA LIAAVHEFND DPDLQDDLSL VELKCAPPPE TKYETPPDEE LKGEETSPKS NLPEFQLELH WGPDQLRDSD PLMILRQWLG SHSVVRNSKE VVFMVLAELF NNALEHGVLG LLSSLKDDDE GFDRYYQERG ARLEKLEDGY VRLQVRLSNT RPARMMVRVS DSGPGFSIKV EDLDCNDESF GRGLPLIKAL CSEFELDGEN ATVKALIELD //