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Database: UniProt
Entry: A0A498RC29_9FIRM
LinkDB: A0A498RC29_9FIRM
Original site: A0A498RC29_9FIRM 
ID   A0A498RC29_9FIRM        Unreviewed;       976 AA.
AC   A0A498RC29;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Phosphotransferase system mannose-type iia component {ECO:0000313|EMBL:VBB08941.1};
GN   ORFNames=LUCI_4227 {ECO:0000313|EMBL:VBB08941.1};
OS   Lucifera butyrica.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Lucifera.
OX   NCBI_TaxID=1351585 {ECO:0000313|EMBL:VBB08941.1, ECO:0000313|Proteomes:UP000277811};
RN   [1] {ECO:0000313|EMBL:VBB08941.1, ECO:0000313|Proteomes:UP000277811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUCI {ECO:0000313|EMBL:VBB08941.1};
RA   Strepis N.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UPPP01000105; VBB08941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498RC29; -.
DR   OrthoDB; 9765164at2; -.
DR   Proteomes; UP000277811; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR004701; PTS_EIIA_man-typ.
DR   InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR002078; Sigma_54_int.
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; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR   SUPFAM; SSF63520; PTS-regulatory domain, PRD; 1.
DR   PROSITE; PS51372; PRD_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_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   Reference proteome {ECO:0000313|Proteomes:UP000277811};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VBB08941.1}.
FT   DOMAIN          130..364
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   DOMAIN          490..594
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          594..723
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000259|PROSITE:PS51096"
FT   DOMAIN          840..976
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  110582 MW;  A06579BCAFF70071 CRC64;
     MKNKLQDIIS LESRKEPYTD MELSERMSVS REYVTLLRKE LNIADSRERK KLYICTEIQE
     ILNSQPTISY RKLSQIMKEK GYGLSRYLLD KYLDEVRSSR GEDSRAEGRE IMPEGQPERE
     SETYQAFANL VGSTGSLEVP IQQAKAAMIY PPNGLHCLIL GETGVGKSEL AEAMYKFAVE
     TGRLKSDSPF IVFNCADYAE NAQLLMSHLF GHVKGAYTGA VGERKGLIEQ AHGGVLFLDE
     VHRLTSEGQE MLFQLIDKGQ FRRLGESEFV RMAKVQLIAA TTENTETTLL ATFKRRIPMI
     IELPSLNKRP LRERLNLITR FFGYESTRMN APIQVRLDVL KALLLYDCLG NIGQLKSDIQ
     VVCAKSFLTY VMDKDEYVKV EVADLSIHVK KGLMKITHKR QEMEALIWQD FIFRPDRYLD
     ANEIDNDIYS FPKEFYSYIE KSYVTYKKQG LNTKEINRIL GSEIERKLQS VIKHVKDNGA
     PISREEIAKV VGAEITAIVE EILKIAEKRL GELDTSIFYC LAIHLHATFN RLDQGREIVN
     PNLDEIKEKF RNEYVVAVEM VEYLKNQWSI DLPDDEVGYI TLYLQGNKKE NEGKVGVLVV
     THGNAGAAML EISNKLLNVN HGQALAMALE ESPTDVLEQL ITLAEAAEEG KGVLLLVDMG
     SLLTFGEIIG ERTGITIETI ERVDTVMVIE GIRRSILPGS KLSDVVSAIE NLNYISKKGR
     VNRRILKRPQ AIITICLTGE GIALHCSRYL KKIFGNQLIG IKLINMGVIG KLDMYKQIQS
     LGNQYDIVAI IGSIDPQYPG IPYISLDDLY HDNSKERILR LLEYSGDSRS SAVNSSLVPA
     VVREAQITLN LQSKNKQDVI KNICDRLLKE GYVKKGYYEA VLKRERMGSF IINQEVVLPH
     ADSSYVNRPT VVIAKMAEPV LWDRNNKVSI VCLLALDIHG KDGVRYLYNK FKDQNILLKL
     KQSQSEQEFK GVLLNE
//
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