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Database: UniProt
Entry: F8CRP5_MYXFH
LinkDB: F8CRP5_MYXFH
Original site: F8CRP5_MYXFH 
ID   F8CRP5_MYXFH            Unreviewed;       748 AA.
AC   F8CRP5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Sensor protein ZraS {ECO:0000256|ARBA:ARBA00039705};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=LILAB_24490 {ECO:0000313|EMBL:AEI66793.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI66793.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI66793.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(2011).
CC   -!- FUNCTION: Member of the two-component regulatory system ZraS/ZraR. May
CC       function as a membrane-associated protein kinase that phosphorylates
CC       ZraR in response to high concentrations of zinc or lead in the medium.
CC       {ECO:0000256|ARBA:ARBA00037481}.
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}.
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DR   EMBL; CP002830; AEI66793.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8CRP5; -.
DR   STRING; 483219.LILAB_24490; -.
DR   KEGG; mfu:LILAB_24490; -.
DR   eggNOG; COG3852; Bacteria.
DR   HOGENOM; CLU_375920_0_0_7; -.
DR   Proteomes; UP000000488; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF54; SENSOR PROTEIN ZRAS; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AEI66793.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:AEI66793.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        31..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          478..694
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          695..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   748 AA;  82098 MW;  4E587E2CFBA973AB CRC64;
     MDIRTQSALL ASIIGLALGV SMLLRPGRPR VLTLYSVFAL TVAGYYLSLF FHNVFPAADY
     PWASRISVGA TILVASLVPG AAVAFFLEFL GVSKGTHLVG RRLALLSAVL GLTVAVTPLA
     DKLWARVCMG VWVLGTLLTY GSLLLHRVRT TESRIEKFRL AYLAIGAGAA ILFSALDFLV
     SFGIPFPTLG SVFSTLYLFF LAHTLLRLRL MDLHELLGKI ASQTVLASIL AAVFTVLTAW
     GKENTGLFLF NTVVAAFVIL ILLEPLKVKV EEMVVRIFFR ERFALLDSLG SLRARMANVI
     EISELARLVL DTLHETGRVT HASVYLLAED RPGYRLLDSR GPLPVAFLDT AVARGLLFAA
     ASGQKAVLRE NVERRMATMR LQVVEGKRYR DELKRLNDTR AALVQVKAGI TVPLMGNDRV
     IGFLNLWDER VPEAFASDEI AIILEVAERL ATVLENSKLY EKIRERDRLA ALGEMAAGLA
     HEIRNPLGAI KGAAQCLDPA QFQGEDAEFL EVIVEEVNRL NGVVTAFLDY ARPMKQSFGT
     TDLNEVVTRT MRLIQNDVPS NLQLAVELDL MLPRVDGDAE QLKQVLINLV QNAVQALGSR
     EGRISVRTEK PERFGELRSA GAEFVEVQVS DNGPGIPPDQ HPHIFVPFYT TKQKGTGLGL
     AICQRIVKNH GGSISVQSKV GEGSTFVIRL PALPTEQPPA SEAPFVEGLP AGTRPSQSLP
     MPDELRDGAR PAQREPRAKR ERRKRLRA
//
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