ID L7CB53_RHOBT Unreviewed; 1347 AA.
AC L7CB53;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RBSWK_05044 {ECO:0000313|EMBL:ELP31045.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP31045.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP31045.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP31045.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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 -!- 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:ELP31045.1}.
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; AMWG01000135; ELP31045.1; -; Genomic_DNA.
DR RefSeq; WP_007339696.1; NZ_AMWG01000135.1.
DR PATRIC; fig|993516.3.peg.5387; -.
DR Proteomes; UP000010959; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000313|EMBL:ELP31045.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:ELP31045.1}.
FT DOMAIN 6..190
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 226..480
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 842..914
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 917..970
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 981..1199
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1218..1334
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 669..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1267
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1347 AA; 150531 MW; 7F45A18371407A69 CRC64;
MEESVPGFAM PSKVVGIGAS AGGLQSLEAL FDELNSETGL AIIVIQHLSP DFDSMMDQLL
SRHSDMPVCL IEDGMYVKPN HIYLLPPGQH VIISNRRLLL AERAKGQSLS FQIDEFFRTL
AQDAGPDSVG IILSGTGTDG SRGVCDIAAA GGMVIVETTE TAAFDGMPRS AYETGVADLV
LSPPEIAKAL HRIAGDDPTI LNGAATRESL DPGQYLESPN RLIFGLLHNT FNIDFSQYKT
EIFSRHIERR LRLAQKASIH DYIELLRTDT DELNQLYSDM LIGPTDFFRD SKAFDRLELD
VFPQLVDDLN PQEDFRCWVA GTATGEEAYT LAIQLAEEFD RRGIEKRIRI FASDVHDPSL
LKAGRGVFTH DRLASITPER LEKYFIERQD GFHVTPEIRK LVVFTPHNVI RDAPFTRLDL
ISCRNLLIYL TPATQQRVLS LFHFGLKTGG VVCLGNSESL GDLRNEFQPL DESLRIYRKF
REISSTAPTG VAIRRPWPAN PPAGTEVARE RTATRQLLKT YDKLLEKFLS PAILINSQKE
ILHVFGGAGA YLSFNDGRPQ NHLLNIILPE LRSALSIALV QLNRDGNPVA IEQIPCSLDG
QQRFVKLTVD KFEIGNERDG TALIQIETQS TQESQLDIDV LTAEQVIAVE YLERELQFTQ
SHLQSTIEEH QSTNEELQST NEQLTASNEE LQSTNEELHS VNEELYTVNA EHQRKIDELT
ELNDDIDNLL TTTNVHTLFL DSRLRLRRFT PRIAELFNLI PQDIGRPINA FTHRLQDPFL
TESIKEVIQT EQFVQREIKD ENGQWYLLRI FPYLSRGTVE GAVVTLVDVT MLQAATEALQ
KSEERFDLAV RGSNAGIWDW KDVTKEAIWC SRRMYALLGR TPTDEMTVSL WEELIHPDDH
ARVMAALNSH LESNTPFDIE YRMEYGTTNE YRWFHMRGSA ERKSGRSETR MAGSFEDVTQ
RREAQQEVKQ GVARRDQFLA MLSHELRNPL GAVTNAIAIM SSEETKPDVT ERALGVVKRQ
LGQMSRLLDD LLDVSRITHG KIELRKQQTD LTKMIEQAVI TTQSRADGAD LELTVALPST
PLIVDGDPAR LEQVTMNLLT NAVKYTPPGG KIRLELKDDG QNAYLEVQDN GAGISSDKLN
EIFSLFYQSD ETLDRSNGGM GVGLTLVKAV VELHDGSVTA KSDGIGCGST FTVTLPLSCN
EVIDANEAPQ SMATKLQSIV LVEDIDDARE MLSGLLELRG LNVYEASDGA AGWNKIREIN
PHAAIIDIGL PVMDGHELAR RIRSDPAHSS IKLVALTGYG QDKDREAVRE SGFDLHLVKP
LNPEKLDQIL TELSEMPTRS PPAQEAI
//
