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Database: UniProt
Entry: A0A0E3ZCI6_9FUSO
LinkDB: A0A0E3ZCI6_9FUSO
Original site: A0A0E3ZCI6_9FUSO 
ID   A0A0E3ZCI6_9FUSO        Unreviewed;       549 AA.
AC   A0A0E3ZCI6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=PTS mannose transporter subunit IIAB {ECO:0000313|EMBL:AKC95687.1};
GN   ORFNames=VC03_04105 {ECO:0000313|EMBL:AKC95687.1};
OS   Sneathia vaginalis.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Sneathia.
OX   NCBI_TaxID=187101 {ECO:0000313|EMBL:AKC95687.1, ECO:0000313|Proteomes:UP000033103};
RN   [1] {ECO:0000313|EMBL:AKC95687.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN35 {ECO:0000313|EMBL:AKC95687.1};
RX   PubMed=23281612;
RG   Vaginal Microbiome Consortium (additional members);
RA   Harwich M.D.Jr., Serrano M.G., Fettweis J.M., Alves J.M., Reimers M.A.,
RA   Buck G.A., Jefferson K.K.;
RT   "Genomic sequence analysis and characterization of Sneathia amnii sp.
RT   nov.";
RL   BMC Genomics 13:S4-S4(2012).
RN   [2] {ECO:0000313|EMBL:AKC95687.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SN35 {ECO:0000313|EMBL:AKC95687.1};
RG   Vaginal Microbiome Consortium;
RA   Harwich M.D.Jr., Serrano M.G., Fettweis J.M., Alves J.M.P., Reimers M.A.,
RA   Buck G.A., Jefferson K.K.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP011280; AKC95687.1; -; Genomic_DNA.
DR   RefSeq; WP_046328793.1; NZ_CP011280.1.
DR   AlphaFoldDB; A0A0E3ZCI6; -.
DR   STRING; 187101.VC03_04105; -.
DR   KEGG; sns:VC03_04105; -.
DR   PATRIC; fig|1069640.6.peg.813; -.
DR   HOGENOM; CLU_012312_1_0_0; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000033103; 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   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   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF20; PTS SYSTEM GLUCOSE-SPECIFIC EIICB COMPONENT-RELATED; 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:UP000033103};
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        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        397..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..432
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          469..549
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        491
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   549 AA;  60132 MW;  E570B4872ECD9098 CRC64;
     MERNKVIVAF EKFGRSFLLP VSVLPAAGIL KGIGAAFTNP STVKMYPFLG VKGLQIFMKL
     LVTLGDVAFK NLPLMFAVGV CVGLAKKEKG SAALSAVLGF LSFHYILNFL LKTTGTLVVA
     DGLTKAQVSQ LMAQSMQTKV LGIQTMDLNV FGGLIVGVVA YFVHKKAITI QLPQVIGFFS
     GPRLVPILIM PVMALVSLIV FIIWPSVQNV INIISVLILK SGYIGTFLYA LAERFLLPFG
     LHHGLNWPIR TTELGGIFNV NGKTVYGTIN AYMAAISTPN GPIDPNITRF SSGKFVYNMF
     GLPGAALAMY KTAKPKNKKI VGSLLLAAAG TSFLTGITEP LEFTFLFVAP MLYAVHAVLA
     GITLLSLHAL GAAFLTPTGH GLINYIIYGV LQGTRTKWYL LPITGVVCFI VYYFVFKFMI
     TKFDYKTPGR EGDIEDIHIS TKEEARSKYG LKTLKDEMRE EKQEKMSTHD QALGLIECYG
     GRENIVTVDA CITRLRIDVK DKAKVDKKRI KEEYHAMGVS ENGMQVQSIY GAHAQTLKME
     IIDILGIED
//
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