ID A0A1Q9JXZ2_9FIRM Unreviewed; 620 AA.
AC A0A1Q9JXZ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=PTS beta-glucoside transporter subunit EIIBCA {ECO:0000313|EMBL:OLR61001.1};
GN ORFNames=BHF69_12285 {ECO:0000313|EMBL:OLR61001.1};
OS Anaerostipes sp. 992a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR61001.1, ECO:0000313|Proteomes:UP000187371};
RN [1] {ECO:0000313|EMBL:OLR61001.1, ECO:0000313|Proteomes:UP000187371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=992a {ECO:0000313|EMBL:OLR61001.1,
RC ECO:0000313|Proteomes:UP000187371};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR61001.1}.
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; MJIG01000005; OLR61001.1; -; Genomic_DNA.
DR RefSeq; WP_075672137.1; NZ_MJIG01000005.1.
DR AlphaFoldDB; A0A1Q9JXZ2; -.
DR STRING; 1261637.BHF69_12285; -.
DR OrthoDB; 92465at2; -.
DR Proteomes; UP000187371; 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; TIGR00830; PTBA; 1.
DR PANTHER; PTHR30175:SF7; NEGATIVE REGULATOR OF SACY ACTIVITY; 1.
DR PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000187371};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 99..457
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 491..595
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 620 AA; 66865 MW; 64E03E5B6E1345C8 CRC64;
MAINHRKCAK EIFDCLGGKE NIVSITHCAT RLRLVVAEYD KVNMEHMEKV DGIKGIFRNN
GQIQLIIGTG SVEKVYEEFL KINKHALVNK KTILEKMMQL LGNIFIPIVP AIVAAGLMMG
CLDVLQTVST TFAGSDWCDI LSLFANTAFL FLPILIAISA AKVFGGNIYL AAIIGIIMVH
PSLINAWDVG KMASTEIPTW NIWFLRIRQI GYQGHVIPVV LVVWLMSKLE KQLHKRIPEV
VDLFVTPLCT VVVGGFLALG IIGPIFSSAE NSIVHLTEYL IAGGNKLGSM IMGTIYPVTV
VTGVHHMYNV VETGMLAKGL NTWMPIVSAA NVAQAAACLA VGMKAKNGKT KAVAIPSAIS
AALGITEPAI FGVNLRLIKP FLCSMIGGGI GAFVAAALHV GATSYGVSGI LGFLITWGFM
FQYGITILVA FASSFVLTWV VWNENPQESD ALSVENILDV VQPEAAAERK REKVIYAPVK
GTIIRREDFS DPIFASGVLG EGVGIEPETG MIVAPLDGMV TSVTDSLHAL GISGPQGMRV
LIQVGVDTVN MKGEGFQLFV TEGEQVRAGQ KLLKFDMNKI HEAGYSTVTA VLVTNSEEYE
SCTVEKTGHT EVMEKLITVQ
//
