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Database: UniProt
Entry: Q8EQQ2
LinkDB: Q8EQQ2
Original site: Q8EQQ2 
ID   LYTS_OCEIH              Reviewed;         585 AA.
AC   Q8EQQ2;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
GN   Name=lytS; OrderedLocusNames=OB1642;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system LytS/LytT that
CC       probably regulates genes involved in cell wall metabolism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BA000028; BAC13598.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EQQ2; -.
DR   SMR; Q8EQQ2; -.
DR   STRING; 221109.gene:10733882; -.
DR   KEGG; oih:OB1642; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OrthoDB; 9776552at2; -.
DR   PhylomeDB; Q8EQQ2; -.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   CDD; cd16924; HATPase_YpdA-YehU-LytS-like; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..585
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000074791"
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          362..580
FT                   /note="Histidine kinase"
FT   MOD_RES         389
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   585 AA;  64669 MW;  931E168546B0605F CRC64;
     MIELTIVLFQ RIGLLLLMAF ILTRIPRFRS LLDKDITLKT VIYHSLIFGL ISIIGAHVGV
     VMIGNELIMQ AWIINVAENE VLIGFSIVVV MIAGLLGGPF LGLGTGMVAG LYIIFLGGGG
     WVANSLINPL AGLLTGWAGQ FFSDDRVMSP NKALFIGIFP PVLHMGLLLI MLPDQQIGVQ
     IVNTIGIPLV VTNSIALTIF TMMIRLALNE TEQEAALETN RALTIAEKAL PLLSEEPGTM
     NARKMAKLLF KELDIAAISI TNRTTVLSHV GLGDDHHQPG EPLKMRLSKK AVKDGRIQIA
     YHQSDIQCGV ENCKLKTAIM VPIYRSGEVI GLINLYYRHS QQITAVEITL AKGLGTIISN
     QISGLEAEKM KKLLKEAKMR NLQAQINPHF LFNTFHLIHS LLRVDAEKAR HILVQLSQFM
     RANLKIASES LVPLHKELEH LQAYLEIVQA RFPDQISTSI HVDDYLLDIE IPPATLQPLV
     ENSIQHGLSL STSKGILTIN ITKTDNNVSI VLLDNGQGFE EKLLPILGKK PLHQNENKGN
     GIALYNINQR LISLLGEDSQ LHIQNTDKGS MVQFILPYRN CKKIM
//
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