ID E2SIB6_9FIRM Unreviewed; 938 AA.
AC E2SIB6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Sigma-54 interaction domain protein {ECO:0000313|EMBL:EFP62728.1};
GN ORFNames=HMPREF0983_00745 {ECO:0000313|EMBL:EFP62728.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP62728.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP62728.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP62728.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFP62728.1}.
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DR EMBL; ACTJ01000017; EFP62728.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SIB6; -.
DR STRING; 658659.HMPREF0983_00745; -.
DR eggNOG; COG1221; Bacteria.
DR eggNOG; COG3933; Bacteria.
DR HOGENOM; CLU_014204_1_1_9; -.
DR BioCyc; EBAC658659-HMP:GMFE-754-MONOMER; -.
DR Proteomes; UP000006223; 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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR002078; Sigma_54_int.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR PANTHER; PTHR32071:SF90; TRANSCRIPTIONAL REGULATORY PROTEIN LEVR; 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; SSF52794; PTS system IIB component-like; 1.
DR SUPFAM; SSF63520; PTS-regulatory domain, PRD; 2.
DR PROSITE; PS51372; PRD_2; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 112..347
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 574..708
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 831..938
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
SQ SEQUENCE 938 AA; 107487 MW; 77413787193D428C CRC64;
MSEQELYDYI YSVITKEYLE NRIQKKEAFG ITAKEVAEHF NTYRSTVSTI LNAAVKDGLF
IKIETRPVLF VPVAILQREL HFTPEKQVYT NEEIKEIFFR KDQDTSDSFS VMIGFDGSQS
LQIKQAQSAI LYPPKGLHTL ITGESGTGKT LFAHTMYEYG RKIKGVSEKE YPFVEFNCAD
YYHNPQLLLS QLFGHIRGAF TGADQETEGL VEKANHGILF LDEIHRLPPE GQELLFYLMD
TGQYRKMGEA NTIRKADILI IGATTENPND VLLKTFKRRI PLTINLPPLR ERPLQEKLKI
MEHLFSKEAI ITQRTYIIDA DIVKAITLYD FTENIGQLAS EIKILCARSF LESKTKEFGE
IKVPYVFLSD NIREAYKKYR KIGYTFTDNY ENYNYDLVIT PSNEISHVKE KVLNEEAYYS
LIEEIRNYSK QGLTSDEVAI RISSAVSSYY DEILNSMYFK TINKDELYKI IEPRIVDFSL
EVMKEIQNRL SVKITEQSIL VLAFHLKFLI DRLRKIKLTE TSSVPAKTGE AIVDDMIDKI
ESKFSLRLPT DEKKFFQLLI KNITSDIVTD NSSKAALYIL AHGNTASSIA EVCNRLLHTD
FVKAFDMPLT QDVNQSYQLF VEEIESLQLK KGVMILADMG SLLDFGHKLT RDTGIPTHTI
PNVSTAIALD FAHIMLNRNE HIDLTYNEYL IKNRFEPAFA TSEKEPAIIS ACSSGRGTSI
AFKNMIEEIL KENSLGYIHV FALSNEELQK KQDAYQEIAN NYNLVAVIGN VHMDVDVPFF
HISELVTDDK KENFIKFLNK TGAGVRPVKN KRVDQNAEEA AGFLAQHVMY VNPLAVQKVS
TEFLNSLFTD LNYDEKNRAS TGFSLIIHIG FMIERIIANK TIIFDHKIPY LEKNKDIFQK
IRTHIKSIEE AFEIEISDDE ICYMMITLYP NTYDTAVA
//
