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Database: UniProt
Entry: A0A0X8G3P1_9FIRM
LinkDB: A0A0X8G3P1_9FIRM
Original site: A0A0X8G3P1_9FIRM 
ID   A0A0X8G3P1_9FIRM        Unreviewed;       551 AA.
AC   A0A0X8G3P1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=PTS transporter subunit IICB {ECO:0000313|EMBL:AMC09497.1};
GN   ORFNames=AT726_11670 {ECO:0000313|EMBL:AMC09497.1};
OS   Turicibacter sp. H121.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Turicibacteraceae; Turicibacter.
OX   NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC09497.1, ECO:0000313|Proteomes:UP000057144};
RN   [1] {ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMC09497.1, ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|EMBL:AMC09497.1,
RC   ECO:0000313|Proteomes:UP000057144};
RX   PubMed=27013036;
RA   Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA   Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT   "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT   the Feces of a Contaminated Germ-Free Mouse.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP013476; AMC09497.1; -; Genomic_DNA.
DR   RefSeq; WP_068759646.1; NZ_JAMQUX010000026.1.
DR   AlphaFoldDB; A0A0X8G3P1; -.
DR   STRING; 1712675.AT726_11670; -.
DR   KEGG; tur:AT726_11670; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000057144; Chromosome.
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; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR011300; PTS_IIBC.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR02003; PTS-II-BC-unk1; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF8; PTS SYSTEM, IIBC COMPONENT; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 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:UP000057144};
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        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..451
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          473..551
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        495
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   551 AA;  58790 MW;  84FFD0DF6809665C CRC64;
     MKKPGFMSFD FWQKFGKALM VVIAVMPAAG IMISLGKLVG MSGGDITVIA TIAKVMEDIG
     WAIIGNLHVL FAVAIGGSWA KERAGGAFAA LIAFILINRI TGALFGVSTA MLADPTATVQ
     SFFGSEMVVS DYFTEVLGAS ALNMGVFVGI ISGFLGASLF NKYYNFNKLP QALAFFNGKR
     FVPFVVIGGS VVTALVLSII WPFAQGALNN FGQWIATSQD TAPILAPFVY GAGERLLLPF
     GLHHMLTIPM NYTELGGTYE ILTGSNAGQI VAGQESLWLA WVTDLNNLKS AGDMEAYNSL
     LNAVTPARFK AGQVILSTAS LMGAAFAMFR NVDSDKKSAY KSMFISAALA TFLTGVSEPL
     EFMFMFISPV LYLCYAILAG LAFALADIIN LRIHAFGMIE FMTRIPMMAN AGLTGDMINF
     VLACLGFFAL NFGVFNFAIK KFKIATPGRL GNYNEEDETQ GEGSTSTTAA SGSQLANDII
     FLLGGAENIV DVDACMTRLR VTVKDSGTVS DQPDWKATGA LGLIIKDNGI QAIYGPKADV
     LKSEIQDILG L
//
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