ID   FRZE_MYXXA              Reviewed;         777 AA.
AC   P18769;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Gliding motility regulatory protein;
DE            EC=2.7.13.3;
GN   Name=frzE;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2165608; DOI=10.1073/pnas.87.15.5898;
RA   McCleary W.R., Zusman D.R.;
RT   "FrzE of Myxococcus xanthus is homologous to both CheA and CheY of
RT   Salmonella typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5898-5902(1990).
RN   [2]
RP   PHOSPHORYLATION AT HIS-49.
RX   PubMed=2123853; DOI=10.1128/jb.172.12.6661-6668.1990;
RA   McCleary W.R., Zusman D.R.;
RT   "Purification and characterization of the Myxococcus xanthus FrzE protein
RT   shows that it has autophosphorylation activity.";
RL   J. Bacteriol. 172:6661-6668(1990).
CC   -!- FUNCTION: FrzE is involved in a sensory transduction pathway that
CC       controls the frequency at which cells reverse their gliding direction.
CC       FrzE seems to be capable of autophosphorylating itself on a histidine
CC       residue and then to transfer that group to an aspartate residue in the
CC       C-terminal part of the protein.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
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DR   EMBL; M35192; AAA25396.1; -; Genomic_DNA.
DR   PIR; A35966; A35966.
DR   RefSeq; WP_011554143.1; NZ_FNOH01000003.1.
DR   AlphaFoldDB; P18769; -.
DR   SMR; P18769; -.
DR   GeneID; 41361459; -.
DR   OMA; MKGEARM; -.
DR   BRENDA; 2.7.13.3; 3551.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProt.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.20.120.160; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
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   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF50341; SSF50341; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..777
FT                   /note="Gliding motility regulatory protein"
FT                   /id="PRO_0000074766"
FT   DOMAIN          1..108
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   DOMAIN          270..509
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          511..645
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   DOMAIN          660..776
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   REGION          129..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         709
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   777 AA;  83190 MW;  9912BD40991C69E5 CRC64;
     MDTEALKKSL LKKFQEVTAD RLQKIQLGVL DLEKETADQA AEDVARELHT MKGEARMLGL
     AAIGQLAHAA EDVLRAEREG KTATEVATDV LLRACDVLSD LNEDLSGANT GNPASEEMVR
     MLAEVSGQTP PAIAGARPVA PPPAPPPAPV AAPVVTPAAV AAPPAPVQAP VAPPPTQAPV
     AEPGAHAAAA APHPAAAHGR DEEAPSAAKS AVADRSIRVN VEVLDALGLL AGDLLVESAR
     GRLRSSETEA LFERFSRLGD RFLRLAEEID ISNEVREQLD RVESDLHMLR DDAFRFVRRN
     DDGINTLHGN LAKMADHVAE ARLVPLSTVF DAFPRAVREM SRTQGKEVDL VIENADIGVD
     RSMLGDVRDA LVHLLRNSVD HGVESPDTRQ QLGKPLNGRI RIRVRVDGDM LHIEVEDDGR
     GIDPERLRQA AISKRLINAV QAAALSEREA IELIFRPGFS TRDQVSELSG RGVGMDVVKR
     KVETLGGSVG VSSRIGRGST ITLRLPQSLA LMKVLLVRLG DDVYGMPAAD VEAVMRVKPD
     DRLEIFGTLA VRHRGKPTAL VALGPLLGLN GGNRFDKPPA VVVRHGEDHA ALVVDGFVDE
     REVAVKPCGG EFLKAAPFIA GTAALEDGRI AVLLHVPDIM AEVRRMARPV TQAPAAKRLR
     VLLVDDSPIA RATEGALVKA LGHSVEEAQD GEEAYVKVQN NTYDLILTDV QMPKLDGFSL
     ARRLKSTPAV ARIPVIILSS LASPEDKRRG LDAGADAYLV KGELGVEVLA QAIDRLT