PTN3B_BACSU
ID PTN3B_BACSU Reviewed; 650 AA.
AC O31645;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PTS system mannose-specific EIIBCA component;
DE AltName: Full=EIIBCA-Man;
DE Short=EII-Man;
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.191;
DE AltName: Full=PTS system mannose-specific EIIB component;
DE Includes:
DE RecName: Full=Mannose permease IIC component;
DE AltName: Full=PTS system mannose-specific EIIC component;
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system mannose-specific EIIA component;
GN Name=manP; Synonyms=yjdD; OrderedLocusNames=BSU12010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP GENE NAME.
RC STRAIN=168;
RX PubMed=10627040; DOI=10.1099/00221287-145-12-3419;
RA Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr., Stuelke J.;
RT "Novel phosphotransferase system genes revealed by genome analysis - the
RT complete complement of PTS proteins encoded within the genome of Bacillus
RT subtilis.";
RL Microbiology 145:3419-3429(1999).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10960106; DOI=10.1128/jb.182.18.5202-5210.2000;
RA Turner M.S., Helmann J.D.;
RT "Mutations in multidrug efflux homologs, sugar isomerases, and
RT antimicrobial biosynthesis genes differentially elevate activity of the
RT sigma(X) and sigma(W) factors in Bacillus subtilis.";
RL J. Bacteriol. 182:5202-5210(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [6]
RP INDUCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF CYS-9.
RX PubMed=20139185; DOI=10.1128/jb.01673-09;
RA Sun T., Altenbuchner J.;
RT "Characterization of a mannose utilization system in Bacillus subtilis.";
RL J. Bacteriol. 192:2128-2139(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-104.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the fructose specific IIb subunit of PTS system from
RT Bacillus subtilis subsp. subtilis str. 168.";
RL Submitted (SEP-2007) to the PDB data bank.
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 mannose transport.
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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
CC -!- INDUCTION: Up-regulated by mannose. Is under the control of ManR. Is
CC subject to carbon catabolite repression (CCR) by glucose. Forms part of
CC an operon with manA and yjdF. {ECO:0000269|PubMed:20139185}.
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. The
CC EIIB domain is also able to transfer its phosphoryl group to a specific
CC histidine residue in ManR, which leads to its inactivation.
CC {ECO:0000255|PROSITE-ProRule:PRU00422, ECO:0000269|PubMed:20139185}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000269|PubMed:20139185}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00417, ECO:0000269|PubMed:20139185}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow with
CC mannose as the sole carbon source. Deletion of manP results in
CC constitutive expression from both the manP and manR promoters,
CC indicating that the phosphotransferase system (PTS) component EII-Man
CC has a negative effect on regulation of the mannose operon and manR.
CC {ECO:0000269|PubMed:10960106, ECO:0000269|PubMed:20139185}.
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DR EMBL; AL009126; CAB13058.2; -; Genomic_DNA.
DR PIR; G69848; G69848.
DR RefSeq; NP_389083.2; NC_000964.3.
DR RefSeq; WP_003245781.1; NZ_JNCM01000035.1.
DR PDB; 2R48; X-ray; 1.80 A; A=2-104.
DR PDBsum; 2R48; -.
DR AlphaFoldDB; O31645; -.
DR SMR; O31645; -.
DR STRING; 224308.BSU12010; -.
DR TCDB; 4.A.2.1.6; the pts fructose-mannitol (fru) family.
DR iPTMnet; O31645; -.
DR jPOST; O31645; -.
DR PaxDb; O31645; -.
DR PRIDE; O31645; -.
DR EnsemblBacteria; CAB13058; CAB13058; BSU_12010.
DR GeneID; 936437; -.
DR KEGG; bsu:BSU12010; -.
DR PATRIC; fig|224308.179.peg.1296; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG1762; Bacteria.
DR InParanoid; O31645; -.
DR OMA; QPIMPII; -.
DR PhylomeDB; O31645; -.
DR BioCyc; BSUB:BSU12010-MON; -.
DR BRENDA; 2.7.1.191; 658.
DR EvolutionaryTrace; O31645; -.
DR Proteomes; UP000001570; Chromosome.
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: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: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; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05569; PTS_IIB_fructose; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
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; IPR004715; PTS_IIA_fruc.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR00848; fruA; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="PTS system mannose-specific EIIBCA component"
FT /id="PRO_0000371313"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 1..98
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 123..456
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 504..649
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 9
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 566
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MUTAGEN 9
FT /note="C->A: Appears to be unable to inactivate ManR, since
FT ManR does not show any decrease in its DNA-binding activity
FT in the presence of this mutant."
FT /evidence="ECO:0000269|PubMed:20139185"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2R48"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2R48"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2R48"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2R48"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2R48"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:2R48"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2R48"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2R48"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2R48"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2R48"
SQ SEQUENCE 650 AA; 69026 MW; BF92BA1E5E7EBE5F CRC64;
MKLLAITSCP NGIAHTYMAA ENLQKAADRL GVSIKVETQG GIGVENKLTE EEIREADAII
IAADRSVNKD RFIGKKLLSV GVQDGIRKPE ELIQKALNGD IPVYRSATKS ESGNHQEKKQ
NPIYRHLMNG VSFMVPFIVV GGLLIAVALT LGGEKTPKGL VIPDDSFWKT IEQIGSASFS
FMIPILAGYI AYSIADKPGL VPGMIGGYIA ATGSFYDSAS GAGFLGGIIA GFLAGYAALW
IKKLKVPKAI QPIMPIIIIP VFASLIVGLA FVFLIGAPVA QIFASLTVWL AGMKGSSSIL
LALILGAMIS FDMGGPVNKV AFLFGSAMIG EGNYEIMGPI AVAICIPPIG LGIATFLGKR
KFEASQREMG KAAFTMGLFG ITEGAIPFAA QDPLRVIPSI MAGSMTGSVI AMIGNVGDRV
AHGGPIVAVL GAVDHVLMFF IAVIAGSLVT ALFVNVLKKD ITASPVLSET APTSAPSEAA
AANEIKQPIQ SQKAEMSEFK KLTDIISPEL IEPNLSGETS DDIIDELIQK LSRRGALLSE
SGFKQAILNR EQQGTTAIGM NIAIPHGKSE AVREPSVAFG IKRSGVDWNS LDGSEAKLIF
MIAVPKESGG NQHLKILQML SRKLMDDNYR ERLLSVQTTE EAYKLLEEIE
