ID A0A2N5N7V4_9BACL Unreviewed; 629 AA.
AC A0A2N5N7V4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=PTS system, beta-glucoside-specific IIB component {ECO:0000313|EMBL:PLT46379.1};
DE EC=2.7.1.191 {ECO:0000313|EMBL:PLT46379.1};
GN ORFNames=B8V81_4810 {ECO:0000313|EMBL:PLT46379.1};
OS Paenibacillus pasadenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT46379.1, ECO:0000313|Proteomes:UP000234789};
RN [1] {ECO:0000313|EMBL:PLT46379.1, ECO:0000313|Proteomes:UP000234789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R16 {ECO:0000313|EMBL:PLT46379.1,
RC ECO:0000313|Proteomes:UP000234789};
RA Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA Delledonne M.;
RT "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT insights on endophytic life style and antifungal activity.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PLT46379.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFEZ01000004; PLT46379.1; -; Genomic_DNA.
DR RefSeq; WP_028596933.1; NZ_NFEZ01000004.1.
DR AlphaFoldDB; A0A2N5N7V4; -.
DR OrthoDB; 9764327at2; -.
DR Proteomes; UP000234789; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR NCBIfam; TIGR00826; EIIB_glc; 1.
DR NCBIfam; TIGR00830; PTBA; 1.
DR PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PLT46379.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..373
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 385..467
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 486..589
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT ACT_SITE 407
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 629 AA; 68483 MW; AACAD2AEC05EE5C4 CRC64;
MNFMGNLQQL GRAVMLPMIV LPAAAICMSL AQLPWDAAGL PAMAEYLQIA GRSLFLFLPY
LFAAGVAWGT SSNGGAASLS ALAGMFIYSG IVQSSSYDIE PTVLIGALIG MLAGYSYERF
KSIRLPESIQ FFGGPRFVPL FVSFVCILFS LFMVAAAPSL SRGLLWLGDV VASAGGFGVF
LYGFLHRILV VFGLHHLLNH VFWFQIGGYR MDGGEMVYGD LPRFFAGDPT AGAFMAGLYP
TMMFALPAIA LAIIQEARED LKPKIKRTFL SAALASFLTG VSEPVEFAFL FVAPYLFVIH
SVLSGLIMWA AYELGIRHGF SFSGGAIDYV INMHLATKGW LLLPLGIVVF LLYYGLFRWA
IRRFQIPTPG REEGSALDEW AGDIPYRAPL ILQAIGGKEN VETLEACITR LRIKVRNDKL
LDNAALRDLG AAGVIRLGGG NVQVVFGTFS ELIREEMLKT MQRDRAQVLF SSPVQGRMIP
LDEVPDPIFA GKLVGDGAAF LPERGELVAP VKGEVILLYP TMHAIGLRTP EGLEVLMHIG
IDTSSLDGYF HAAVKEGDEV IPGQLLISFD IQRLRKAGKS LATPMLITNP QLVRSWGFGP
FKTVKRGQTA VMSVMLRESK DSQAGGKRS
//