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Database: UniProt
Entry: A4G8Q2_HERAR
LinkDB: A4G8Q2_HERAR
Original site: A4G8Q2_HERAR 
ID   A4G8Q2_HERAR            Unreviewed;       478 AA.
AC   A4G8Q2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Type 4 fimbriae expression regulatory protein {ECO:0000313|EMBL:CAL62889.2};
GN   Name=pilR {ECO:0000313|EMBL:CAL62889.2};
GN   OrderedLocusNames=HEAR2772 {ECO:0000313|EMBL:CAL62889.2};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62889.2, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL62889.2, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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DR   EMBL; CU207211; CAL62889.2; -; Genomic_DNA.
DR   AlphaFoldDB; A4G8Q2; -.
DR   STRING; 204773.HEAR2772; -.
DR   KEGG; har:HEAR2772; -.
DR   eggNOG; COG2204; Bacteria.
DR   HOGENOM; CLU_000445_0_6_4; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   PANTHER; PTHR32071:SF100; RESPONSE REGULATOR PROTEIN PILR; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          8..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..371
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   478 AA;  51642 MW;  E359A788429EEB06 CRC64;
     MRAMTSPRIL VVDDEADLRE LLEITLIKMG LDIDSAATLE AARDYLAKTE YALVLTDMRL
     PDGLGIELVQ EVTAQYKNTP IAVITAFGSA DNAVIALKAG AFDYLSKPVG LEQLRVMVRS
     ALRISQGVVS DKVNQKAIAP TALRLMGQSD AMQALRAQIA RLARSMAPVA ISGESGSGKE
     LAARDIHAQS ARNDKPFVAV NCGAIPEALM EAEFFGYRKG AFTGAADDRD GFFQAANGGT
     LLLDEVADLP LAMQVKLLRA IQERCVRKVG ATVEEPVDVR IISATHQNLH DCVGKGTFRQ
     DLYYRLNVIE LHLPPLRERL DDIGLLAQAI LVRLGGGEQA ALSPAALAAL CSYSFPGNVR
     ELENILERAL AFANDGLIEV ADLALKASPS LNPAPASTPS AVSQPISSEV EAEALATLVA
     SSDIPESLPD HLDEVEREII RRALAKTRFN RTQAAELLGI SFRQLRYRMQ RLDINAPE
//
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