PTFBC_RHOCA
ID PTFBC_RHOCA Reviewed; 578 AA.
AC P23387;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=PTS system fructose-specific EIIB'BC component {ECO:0000305|PubMed:2254279};
DE AltName: Full=EIIB'BC-Fru {ECO:0000305|PubMed:2254279};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:2254279};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2254279};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000303|PubMed:2254279};
DE AltName: Full=Fructose permease IIC component {ECO:0000303|PubMed:2254279};
GN Name=fruA {ECO:0000303|PubMed:2254279};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=2254279; DOI=10.1128/jb.172.12.7167-7178.1990;
RA Wu L.-F., Saier M.H. Jr.;
RT "Nucleotide sequence of the fruA gene, encoding the fructose permease of
RT the Rhodobacter capsulatus phosphotransferase system, and analyses of the
RT deduced protein sequence.";
RL J. Bacteriol. 172:7167-7178(1990).
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 FruAB PTS system is involved in fructose transport.
CC {ECO:0000250|UniProtKB:P20966, ECO:0000305|PubMed:2254279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC fructose 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC ChEBI:CHEBI:64837; EC=2.7.1.202;
CC Evidence={ECO:0000250|UniProtKB:P20966};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P20966, ECO:0000255|PROSITE-ProRule:PRU00427};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P20966,
CC ECO:0000255|PROSITE-ProRule:PRU00427}.
CC -!- INDUCTION: By fructose. {ECO:0000250|UniProtKB:P23355}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- DOMAIN: In the N-terminal, the PTS system fructose-specific possesses a
CC duplicated EIIB domain (EIIB' domain) which lacks the active site and
CC functions to facilitate phosphoryl transfer between the EIIA domain of
CC diphosphoryl transfer protein (DTP) and the EIIB domain. The presence
CC of the EIIB' domain is required for normal high affinity recognition of
CC DTP by the PTS system fructose-specific as well as for normal rates of
CC phosphoryl transfer between the EIIA and EIIB domains of DTP and PTS
CC system fructose-specific, respectively. {ECO:0000250|UniProtKB:P20966}.
CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00427}.
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DR EMBL; X53150; CAA37303.1; -; Genomic_DNA.
DR PIR; B37852; B37852.
DR RefSeq; WP_013068250.1; NZ_VIBE01000014.1.
DR AlphaFoldDB; P23387; -.
DR GeneID; 31491368; -.
DR OMA; CKLMAPH; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR GO; GO:0090582; F:protein-phosphocysteine-D-fructose-phosphotransferase system transporter activity; ISS:UniProtKB.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05569; PTS_IIB_fructose; 2.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 2.
DR SUPFAM; SSF52794; SSF52794; 2.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 2.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Repeat; Sugar transport; Transferase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..578
FT /note="PTS system fructose-specific EIIB'BC component"
FT /id="PRO_0000186513"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 1..99
FT /note="PTS EIIB type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 119..214
FT /note="PTS EIIB type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 241..576
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 125
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT MOD_RES 125
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 578 AA; 58576 MW; 87793E5AAA608E4E CRC64;
MSKIVAVTAG AKGVAHTHLA AEALSATAQA LGHQIRVERH SAEGVEAPLQ GAEIAAADVV
LIAADLRIED VRFVTKPVYR TSTARAVTQT AAVLAEALAL TGEETPQMTT DTGQRPLRVV
AITSCPTGIA HTFMAADALK KTAAARGWEI AVETQGSVGS QNALSAAQIQ AADLVVIAAD
THVDDSRFAG KKVYKTSVGA AVKGAAKVLD AALAEGVVLG TNLADTVDAL KAQRAATRSG
PYMHLLTGVS YMLPLVVAGG LLIALSFVFG IKAFEVEGTL PAALMAIGGG AAFKLMVPVL
AGFIAYSIAD RPGLTPGLIG GMLAVNLNAG FLGGIVAGFL AGYVARWLRD AIKLPRTLEG
LKPVLILPLL STAITGLIMV YVVGTPVAAI LAAMTAFLQG LGTTNAVVLG LILGGMMAVD
MGGPINKAAY TFAVGLLTSS TYAPMAAVMA AGMTPPLGLA LATLVAKNRF TAEEREAGGA
AAVLGLSFIT EGAIPFAAKD PARVIPSIIV GSAITGALSM ALGCLLVAPH GGIFVLAIPH
AVTNLGLYAL SIVVGTLVTT GLLIALKKPI PAEERARS
