ID K9EWJ6_9LACT Unreviewed; 512 AA.
AC K9EWJ6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=PTS system, alpha-glucoside-specific IIBC component {ECO:0000313|EMBL:EKU93600.1};
GN ORFNames=HMPREF9698_00895 {ECO:0000313|EMBL:EKU93600.1};
OS Alloiococcus otitis ATCC 51267.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alloiococcus.
OX NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU93600.1, ECO:0000313|Proteomes:UP000009875};
RN [1] {ECO:0000313|EMBL:EKU93600.1, ECO:0000313|Proteomes:UP000009875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU93600.1,
RC ECO:0000313|Proteomes:UP000009875};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL Submitted (SEP-2012) 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:EKU93600.1}.
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DR EMBL; AGXA01000018; EKU93600.1; -; Genomic_DNA.
DR AlphaFoldDB; K9EWJ6; -.
DR STRING; 883081.HMPREF9698_00895; -.
DR PATRIC; fig|883081.3.peg.892; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_9; -.
DR Proteomes; UP000009875; 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; 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; IPR010975; PTS_IIBC_a_glc.
DR NCBIfam; TIGR00826; EIIB_glc; 1.
DR NCBIfam; TIGR02005; PTS-IIBC-alpha; 1.
DR PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR30009:SF12; PHOSPHOTRANSFERASE IIC COMPONENT GLVC; 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; 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:UP000009875};
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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..413
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 436..512
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 458
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 512 AA; 56420 MW; B66F2A5840852877 CRC64;
MQKIQRFGGA MITPVLLFAF NGLMLALSIA FQNPDIVGSI ANEGTFWNNI WSVIEQGGWV
VFNHMEILFV LGLPIGLAKK AQARAALEAF VIYMTWNTFI NAMMTTWNFG VDLTDAEGIG
VKQIAGVVTL DTNIIGAILI SAVAIWLHNH FFDTPLPEWL GIFSGSSFVV ILGFFLALPL
AYLTAVIWPP IQELIFQLQG VMATSGTLGV GIYVFLEKIL IPTGLHHFIY QPFEFGPAVV
EGGLVARWFE MLPEIASFEG PLRQIFPAGG FFFQNASKLF YPIGIGAAFI ATAKPERRKQ
TLALIIPTAL TAILTGITEP FEFTFLFLAP QLFLVHALLT ATFAMTIYSL GVAGNIGGGL
IGHISGFALP LINNHLDSLL IYYGAGLVFI FIYFAVFRFA ILRFDIKTPG RELDGEAVRM
YSKSDYKEKQ RANPNQEKAI QFLRGLGGKE NIKEVTNCVS RLRLIVKDES IVEDDQFFKA
AGAHGVVRNG SGIQIVVGME VPKVREFFDE LL
//
