PTYBC_VIBCH
ID PTYBC_VIBCH Reviewed; 481 AA.
AC Q9KVD9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=EIIBC-MurNAc {ECO:0000250|UniProtKB:P77272};
DE Includes:
DE RecName: Full=N-acetylmuramic acid-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P77272};
DE EC=2.7.1.192 {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIB component {ECO:0000250|UniProtKB:P77272};
DE Includes:
DE RecName: Full=N-acetylmuramic acid permease IIC component {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIC component {ECO:0000250|UniProtKB:P77272};
GN Name=murP; OrderedLocusNames=VC_0207;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000250|UniProtKB:P77272}.
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:0000250|UniProtKB:P77272};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93383.1; ALT_INIT; Genomic_DNA.
DR PIR; H82352; H82352.
DR RefSeq; NP_229864.1; NC_002505.1.
DR RefSeq; WP_001074155.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVD9; -.
DR SMR; Q9KVD9; -.
DR STRING; 243277.VC_0207; -.
DR DNASU; 2614844; -.
DR EnsemblBacteria; AAF93383; AAF93383; VC_0207.
DR KEGG; vch:VC_0207; -.
DR PATRIC; fig|243277.26.peg.188; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; FGIHQGF; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0090588; F:protein-phosphocysteine-N-acetylmuramate phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 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 Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..481
FT /note="PTS system N-acetylmuramic acid-specific EIIBC
FT component"
FT /id="PRO_0000186673"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 122..481
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 481 AA; 50263 MW; 9F2E872C71C54863 CRC64;
MAKITQTMMA QVLSLVGGSG NVAKCGNCMT RLRLTLNNSA LADHAALKKI SGVMGVVESD
AQLQIILGPG KAQTAADMMN ALIESGDNVA PAVSEADLST IAAQQKKQMK SKQTSAVQRF
LSKFATIFTP LIPGFIAAGL LLGIATLLEQ IYVVGQTPSE FMLDLVAYLK VFGKGLFAFL
SILIGYNAQQ AFGGSGVNGA ILASLFVLGY DPEATKGIYS GMSEFFGFAI DPRGNIIGVL
LAAILGAQVE RKVREYMPDD LDMILTSVVT LLIMGAVTFL IIMPIGGELF KGMSWLFLNL
NDNPLGAAIL AGLFLISVVF GIHQGFVPVY FALMEAQGFN SLFPILAMAG AGQVGASLAL
YARAKKETTI RTQIKGAIIP GILGIGEPLI YGVTLPRVKP FVTACIGGAA GGFFIGLISY
LGLPVGLNTV FGPSGVVAIP LMTSADGIFA GMAVFVGGLL ISYTVGFAAT YFFGCKDVDL
S
