ID A0A221M9H8_9BACI Unreviewed; 656 AA.
AC A0A221M9H8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ASN04295.1};
GN ORFNames=CFK40_04360 {ECO:0000313|EMBL:ASN04295.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN04295.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN04295.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN04295.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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DR EMBL; CP022437; ASN04295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221M9H8; -.
DR KEGG; vne:CFK40_04360; -.
DR OrthoDB; 3710983at2; -.
DR Proteomes; UP000204391; Chromosome.
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; cd05568; PTS_IIB_bgl_like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.1790.10; PRD domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR013196; HTH_11.
DR InterPro; IPR007737; Mga_HTH.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR30185; CRYPTIC BETA-GLUCOSIDE BGL OPERON ANTITERMINATOR; 1.
DR PANTHER; PTHR30185:SF13; LICABCH OPERON REGULATOR-RELATED; 1.
DR Pfam; PF08279; HTH_11; 1.
DR Pfam; PF05043; Mga; 1.
DR Pfam; PF00874; PRD; 2.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF52794; PTS system IIB 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; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 192..297
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
FT DOMAIN 305..413
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
FT DOMAIN 420..511
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 515..655
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
SQ SEQUENCE 656 AA; 74703 MW; FE5824C6AB111155 CRC64;
MLAHLNKRML KALKLLSKTN DYLSSIHLSQ KMGVTSRTVR EDIKNLNHIL KEYSIFIDSS
RGNGFKLSNS SGELNTLINQ FENVLSDNDF NPIMPEDRVR YMIKKLLYSP ESIKIQAFVE
DLYVSESTIK NDIQRAKLIL NKYNISISKD NKGLYVEGHE LNKRFCISDY LIHSSAIDDR
LILSFINNNS YIISDSDLVK IKSTILYYLN EENMVISDFA LKKIAVHIAI VISRIKTGQY
IDLKSEDFSN LTNEGEYRIS GEIVKAIGKE FKMSFSQDET VYMTMHLVGN RISQAGGIPT
DLLNYLGEDI YKLSYKILNE VGSWIKEIDL KKEKEFVYSL GLHLKQLLHR LSFNMNIRNP
MLSIIKIKYP LAFEAGVVSA KTIMKETGFQ INENEIGFLA LHFGVVIEKQ RLQTLSTKKK
KIALVCASGM ATSELLLTKL SHILGSNYYM IGTYALHQID ELTNQQPDII LTTVPIEEEV
SIPILIVPSI LDDSDIDSIK GSLTKLEGET SSISQFIKED LFFQSLTITT KHEALQFLTE
KMIDKGYIND KIKQSILARE NISSTAIGNM VAIPHPLEVE MNQSCICTAI LEHEIPWNAG
EDVSIIFIIV LEEKWRPKFQ EIFIGLYDII HSSDNVLTLS KQKNFYDFIG MINSMK
//