PTNAB_STRP6
ID PTNAB_STRP6 Reviewed; 330 AA.
AC Q5XAF5; P82545;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=PTS system mannose-specific EIIAB component {ECO:0000250|UniProtKB:P69797};
DE EC=2.7.1.191 {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=EIIAB-Man {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=EIII-Man {ECO:0000250|UniProtKB:P69797};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=PTS system mannose-specific EIIA component {ECO:0000250|UniProtKB:P69797};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=PTS system mannose-specific EIIB component {ECO:0000250|UniProtKB:P69797};
GN Name=manX {ECO:0000250|UniProtKB:P69797}; OrderedLocusNames=M6_Spy1473;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1] {ECO:0000312|EMBL:AAT87608.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2]
RP PROTEIN SEQUENCE OF 13-30; 132-169; 197-211; 241-280; 300-310 AND 319-326.
RC STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
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. The
CC enzyme II ManXYZ PTS system is involved in mannose transport.
CC {ECO:0000250|UniProtKB:P69797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837;
CC EC=2.7.1.191; Evidence={ECO:0000250|UniProtKB:P69797};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P69797}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69797}. Cell
CC membrane {ECO:0000250|UniProtKB:P69797}.
CC -!- DOMAIN: The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-4 domain. {ECO:0000250|UniProtKB:P69797, ECO:0000305}.
CC -!- DOMAIN: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on
CC a histidyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00424}.
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DR EMBL; CP000003; AAT87608.1; -; Genomic_DNA.
DR RefSeq; WP_011184868.1; NC_006086.1.
DR AlphaFoldDB; Q5XAF5; -.
DR SMR; Q5XAF5; -.
DR EnsemblBacteria; AAT87608; AAT87608; M6_Spy1473.
DR KEGG; spa:M6_Spy1473; -.
DR HOGENOM; CLU_074797_0_0_9; -.
DR OMA; EMIFGKQ; -.
DR Proteomes; UP000001167; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00006; PTS_IIA_man; 1.
DR CDD; cd00001; PTS_IIB_man; 1.
DR Gene3D; 3.40.35.10; -; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF03830; PTSIIB_sorb; 1.
DR SUPFAM; SSF52728; SSF52728; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Kinase; Membrane;
KW Phosphoprotein; Phosphotransferase system; Sugar transport; Transferase;
KW Transport.
FT CHAIN 1..330
FT /note="PTS system mannose-specific EIIAB component"
FT /id="PRO_0000259407"
FT DOMAIN 2..130
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 166..330
FT /note="PTS EIIB type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT REGION 143..161
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 181
FT /note="Pros-phosphohistidine intermediate; for EIIB
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT SITE 91
FT /note="Involved in the phosphoryl transfer between H-10 and
FT H-175"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT MOD_RES 10
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT MOD_RES 181
FT /note="Phosphohistidine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P69797,
FT ECO:0000255|PROSITE-ProRule:PRU00424"
FT CONFLICT 304
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35582 MW; 0FEC677C80126E30 CRC64;
MGIGIIIASH GKFAEGIHQS GSMIFGEQEK VQVVTFMPNE GPDDLYGHFN NAIQQFDADD
EILVLADLWS GSPFNQASRV AGENPDRKMA IITGLNLPML IQAYTERLMD AGAGIEQVAA
NIIKESKDGI KALPEDLNPV EETAATEKVV NALQGAIPAG TVIGDGKLKI NLARVDTRLL
HGQVATAWTP ASKADRIIVA SDEVAQDDLR KQLIKQAAPG GVKANVVPIS KLIEASKDPR
FGNTHALILF QTPQDALRAV EGGVEINELN VGSMAHSTGK TMVNNVLSMD KEDVATFEKL
RDLSVTFDVR KVPNDSKKNL FELIQKANIK
