ID   HLYX_ACTPL              Reviewed;         240 AA.
AC   P23619;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Regulatory protein HlyX;
GN   Name=hlyX;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2198268; DOI=10.1128/jb.172.8.4587-4592.1990;
RA   Macinnes J.I., Kim J.E., Lian C.J., Soltes G.A.;
RT   "Actinobacillus pleuropneumoniae hlyX gene homology with the fnr gene of
RT   Escherichia coli.";
RL   J. Bacteriol. 172:4587-4592(1990).
CC   -!- FUNCTION: Confers a hemolytic phenotype on E.coli. May regulate, rather
CC       than mediate, hemolytic activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Possesses 4 cysteines which may bind a metal ion
CC       (possibly iron).
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DR   EMBL; M80712; AAA21920.1; -; Genomic_DNA.
DR   PIR; A37769; A37769.
DR   AlphaFoldDB; P23619; -.
DR   SMR; P23619; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00092; HTH_CRP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR012318; HTH_CRP.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00325; Crp; 1.
DR   PRINTS; PR00034; HTHCRP.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   4: Predicted;
KW   Activator; Cytolysis; Cytoplasm; DNA-binding; Hemolysis; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..240
FT                   /note="Regulatory protein HlyX"
FT                   /id="PRO_0000100181"
FT   DOMAIN          163..236
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        196..215
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   REGION          15..28
FT                   /note="Essential for the oxygen-regulated activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  27107 MW;  C11E5F2CFDCA58C8 CRC64;
     MKIVSDAKHT GRTRCTIHCQ NCSISQLCLP FTLSEHELTQ LDNIIERKKP VQKSQIIFQS
     GDELRSIYAI RSGTIKSYTI SESGEEQITA FHLPGDLVGF DAIMNMKHVG FAQALETSMI
     CEIPFDILDD LAGKMPKIRH QIMRLMSNEI KSDQEMILLL SKMSAEEKLA AFLHNLSQRY
     AAPGFSAREF RLTMTRGDIG NYLGLTIETI SRLLGRFQKS GMITVQGKYI TINRMDELTV
//