ID A0A1Q9HKP9_9VIBR Unreviewed; 482 AA.
AC A0A1Q9HKP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000256|ARBA:ARBA00040399};
DE EC=2.7.1.192 {ECO:0000256|ARBA:ARBA00039021};
DE AltName: Full=EIIBC-MurNAc {ECO:0000256|ARBA:ARBA00043021};
GN ORFNames=BIY22_18970 {ECO:0000313|EMBL:OLQ90980.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ90980.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ90980.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ90980.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in N-acetylmuramic acid (MurNAc) transport, yielding
CC cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic
CC acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably
CC because of the 1,6-anhydro ring. {ECO:0000256|ARBA:ARBA00037346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-
CC muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-
CC phosphate(in); Xref=Rhea:RHEA:33399, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:58721, ChEBI:CHEBI:64837,
CC ChEBI:CHEBI:64848; EC=2.7.1.192;
CC Evidence={ECO:0000256|ARBA:ARBA00036529};
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:OLQ90980.1}.
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DR EMBL; MJMJ01000011; OLQ90980.1; -; Genomic_DNA.
DR RefSeq; WP_075707271.1; NZ_MJMJ01000011.1.
DR AlphaFoldDB; A0A1Q9HKP9; -.
DR STRING; 1381081.BIY22_18970; -.
DR OrthoDB; 9797715at2; -.
DR Proteomes; UP000186313; 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 PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-SPECIFIC EIIBC 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 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 121..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..474
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 123..482
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 482 AA; 50666 MW; D3401142835B1634 CRC64;
MAKINTNTMK DILAAVGGGG NIVKAGNCMT RLRLTLTDFG KVDKETLNAM GAVMGVVESD
EQLQIIMGPG KAQQASEMMN ELLEGLLGDD AEEKPEQDLA SIAKQQKSQV KSKQTSAVQR
FLSKFATIFT PLIPGFIAAG LLLGIATLIE QTMIVGQDAS SFIISLVAYM KIFGKGLFAF
LSILIGYNAQ QAFGGSGVNG AILASLFVLG YNPEATSGIY SGMSDFFGFA IDPRGNIIGV
LLAAIIGAKV ERIVRQYMPD DLDMILTSVV TLLIMGAVTF IVIMPVGGVL FKGMSWLFLN
LNDNPLGAAI LAGLFLISVV FGIHQGFVPV YFALMEAQGF NSLFPILAMA GAGQVGASLA
LYWKSDKSSV LRTQIRGAII PGILGIGEPL IYGVTLPRVK PFVTACIGGA AGGFFIGLIS
YLGLPVGLNT VFGPSGIVAI PLMTSNEGIF LGMAVFVCGL VVSYVAGFFA TLLFGTKDID
LS
//