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Database: UniProt
Entry: A0A1M6PGF3_9CLOT
LinkDB: A0A1M6PGF3_9CLOT
Original site: A0A1M6PGF3_9CLOT 
ID   A0A1M6PGF3_9CLOT        Unreviewed;       899 AA.
AC   A0A1M6PGF3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Sigma 54 modulation protein {ECO:0000313|EMBL:SHK07029.1};
GN   ORFNames=SAMN02745912_02145 {ECO:0000313|EMBL:SHK07029.1};
OS   Paramaledivibacter caminithermalis DSM 15212.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Paramaledivibacter.
OX   NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHK07029.1, ECO:0000313|Proteomes:UP000184465};
RN   [1] {ECO:0000313|EMBL:SHK07029.1, ECO:0000313|Proteomes:UP000184465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15212 {ECO:0000313|EMBL:SHK07029.1,
RC   ECO:0000313|Proteomes:UP000184465};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRAG01000024; SHK07029.1; -; Genomic_DNA.
DR   RefSeq; WP_073149696.1; NZ_FRAG01000024.1.
DR   AlphaFoldDB; A0A1M6PGF3; -.
DR   STRING; 1121301.SAMN02745912_02145; -.
DR   OrthoDB; 9765164at2; -.
DR   Proteomes; UP000184465; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd00006; PTS_IIA_man; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR   Gene3D; 1.10.1790.10; PRD domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR004701; PTS_EIIA_man-typ.
DR   InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR   InterPro; IPR033887; PTS_IIA_man.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR32071:SF38; PSP OPERON TRANSCRIPTIONAL ACTIVATOR; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF03610; EIIA-man; 1.
DR   Pfam; PF00874; PRD; 2.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR   SUPFAM; SSF63520; PTS-regulatory domain, PRD; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51372; PRD_2; 2.
DR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          83..317
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   DOMAIN          441..546
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          550..681
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000259|PROSITE:PS51096"
FT   DOMAIN          796..899
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
SQ   SEQUENCE   899 AA;  102835 MW;  4EBFFE7FD6FE6527 CRC64;
     MKKVNQVYEA LVELEKKNKR GISAKEISEV LNTDRANVSR YLNMLYRDNR VAKIEGRPVL
     YKSIKSDLIQ RTTMGNKNSL NKIIGAKASL RTPIQQARAA ILYPPNGLHT LILGETGVGK
     SMFAELMYQF AKESKIIEED APFIQFNCAD YAENPQLIMS QIFGVKKGAY TGADCDKEGL
     LKKADRGILF LDEVHRLSPQ GQEMLFTFID KGYFRPLGET EKVIYVDVRI IAATTEDPQS
     YLLKTFTRRI PMTIVLPALR DKGMAERYEL IESCIKRESK RIGKSIYVNR NSLISLLLYD
     CPNNIGQLKS DIQLACAKAF VKYKSKEEKY ILISQSDLPQ HVKRGLMKIQ NNREEIDRIF
     KGKGDILRFY YKDDKDHNIS PQYQVSKGFY DVIEKKLEAL KNAGIEDKEI DNIINLAIES
     HFRKYIENLP KGIEKNEISE IVDIEILKVV EEILNFAGKR LKREYDEKIY FGLALHLHGC
     IERLQSGNKI YNPKLNMIRV DYPNEFVVAM EIARIIDDKF NIETPLDEIG YLTMFLASNT
     LGIRDEEKAK VGILVIMHGK STASSMVEVV NNLVGGQHAK ALDMPLNMKP QTMYEIAKQH
     IKEMDRGKGI IVMVDMGSLT NFGDMIYEET GIIVKTIDMV STPIVINACR KAILGQDLNE
     IYTTCKQMNL SNKATARREN INDKNIIITA CFTGEGASER LKRIIEDKLY EKNSIEIIPL
     NILDRREFLC KIDQYREKHK ILAVVSTIDI NLNDIQCISA AEVLKGEGIK KIINIVKEED
     LYLNIGKSLK EHMMYIDGKK IVDDVRYIVD SIEESLNIQV VAEVKVGIIL HLSFLIDKLC
     GNGKETHFED LEEYKNQYSR ELIIIKDCLR SLESNYNIEI GENELAYICK MFMLNKEDI
//
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