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Database: UniProt
Entry: M1P6R6_9CORY
LinkDB: M1P6R6_9CORY
Original site: M1P6R6_9CORY 
ID   M1P6R6_9CORY            Unreviewed;       686 AA.
AC   M1P6R6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=PTS system mannose-specific transporter subunit IIBCA {ECO:0000313|EMBL:AGF72351.1};
GN   ORFNames=A605_06745 {ECO:0000313|EMBL:AGF72351.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72351.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF72351.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72351.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA   Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT   type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003697; AGF72351.1; -; Genomic_DNA.
DR   RefSeq; WP_015400770.1; NZ_JIAJ01000015.1.
DR   AlphaFoldDB; M1P6R6; -.
DR   STRING; 1121362.A605_06745; -.
DR   KEGG; chn:A605_06745; -.
DR   PATRIC; fig|1121362.3.peg.1362; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_2_1_11; -.
DR   OrthoDB; 9797715at2; -.
DR   Proteomes; UP000011723; 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; 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; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF1; PTS SYSTEM ARBUTIN-, CELLOBIOSE-, AND SALICIN-SPECIFIC EIIBC COMPONENT-RELATED; 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; PS00371; PTS_EIIA_TYPE_1_HIS; 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:UP000011723};
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        125..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..461
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          116..473
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          552..656
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51093"
FT   REGION          477..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        28
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   686 AA;  72936 MW;  D8E288E5F33CC903 CRC64;
     MASKTASTSQ HIITEIGGAD NVTSLTHCAT RLRFQLHDQS KVDVDSLEKD PAVLGVVKQG
     TTGLQVVMGG GVAEYYQAIM KEPAMRQVGD GESSAPKKKE YEGVRGKYSW VDYSFEFLSD
     TFRPILWALL GASLIITLLV LADTFGLQDF RAEEQPPTYQ FLHAMWNSVF YFLPIFVGAT
     AARKLGANEW VGAAIPAALL TPQFLALGEA GETITVFGLP LTLNDYSSQV FPPLIAAIGL
     YWVEKGLKKL IPASVQMVFV PFFSLLIMIP ATAFLLGPFG IGVGNGISNL LEAIYNFSPF
     ILAIVIPLLY PFLVPLGLHW PLNAIMIQNI ATLGYDFIQG PMGAWNFACF GVVAGVMVIS
     LRERNNQMRQ VSLGGLMAGL LGGISEPSLY GVLLRFKKTY FRLLPGCFAG GVVMGFVQPE
     TSAFVFTSVL TIAAFTPMIG YTIGVLVAFV TSFLLVIFLD YRGKDERAEI RAQLAAEREA
     ANREEDERID AAEDAGTTPA PAPTPEDGAA GTAVATAAAP AKEVKPALRP GAVTEIGAPL
     AGRAIALSEV PDPAFAGGAL GQGIAIEPSG DSVVAPADGS IITVQKTGHA VGLRLDNGIE
     MLIHIGIDTV QMGGEGFEVH VGKKQRVSAG DVLITFDRDA ITAAGYPAVT PVLIANTKKF
     ATVEAHPAEH ADLGDKVITV FAKQGE
//
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