PTMCB_STAS1
ID PTMCB_STAS1 Reviewed; 508 AA.
AC Q49ZA3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000250|UniProtKB:P28008};
DE AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE Includes:
DE RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN Name=mtlA; OrderedLocusNames=SSP0728;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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 CmtAB PTS system is involved in D-mannitol transport.
CC {ECO:0000250|UniProtKB:P28008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannitol 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC ChEBI:CHEBI:64837; EC=2.7.1.197;
CC Evidence={ECO:0000250|UniProtKB:P00550,
CC ECO:0000250|UniProtKB:P28008};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
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}.
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}.
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DR EMBL; AP008934; BAE17873.1; -; Genomic_DNA.
DR RefSeq; WP_011302638.1; NZ_MTGA01000032.1.
DR AlphaFoldDB; Q49ZA3; -.
DR SMR; Q49ZA3; -.
DR STRING; 342451.SSP0728; -.
DR EnsemblBacteria; BAE17873; BAE17873; SSP0728.
DR KEGG; ssp:SSP0728; -.
DR PATRIC; fig|342451.11.peg.730; -.
DR eggNOG; COG2213; Bacteria.
DR HOGENOM; CLU_028721_2_1_9; -.
DR OMA; GWAIKRF; -.
DR OrthoDB; 554815at2; -.
DR Proteomes; UP000006371; Chromosome.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter 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; cd05567; PTS_IIB_mannitol; 1.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR029503; PTS_EIIB_mannitol.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004718; PTS_IIC_mtl.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR TIGRFAMs; TIGR00851; mtlA; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="PTS system mannitol-specific EIICB component"
FT /id="PRO_0000186628"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 53..56
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 78..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 142..163
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 164..172
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 194..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 301..320
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 343..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 19..351
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 420..508
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT REGION 355..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008"
FT MOD_RES 426
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT ProRule:PRU00422"
SQ SEQUENCE 508 AA; 54700 MW; 33926C8EA2CE175D CRC64;
MSQTETQENK GLGRKVQAFG SFLSSMIMPN IGAFIAWGFI AAIFIDGGWW PNKDLSELAG
PMISYLIPLL IAYSGGRLIH EMRGGIIAAV ATMGVIVALP DTPMLLGAMI MGPLVGWLMK
KTDEFIQPRT PQGFEMLFNN FSAGILGFIM TIVGFKILAP IMEFIMHILS LAVEALVHAH
LLPLVSIIVE PAKIVFLNNA INHGVFTPLG ADQAASAGQS ILYTIESNPG PGLGILVAYM
IFGKGTAKAT SYGAGIIHFL GGIHEIYFPY VLMRPLLFIA VILGGMTGVA TYSLLDFGFK
SPASPGSFIV YMLNAPKGEF LHMVLGVLLA AIVSFIVAAL ILKFTKEPEE DLEAATEKME
ASKGKKSSVS SKLKGNEDNN ATSTTASTST SENNEEQSEE ALLDNYDTEN VDAHDYSKVN
HVIFACDAGM GSSAMGASML RNKFKKAGIQ DVNVTNTAIN QLPSDAQLVI TQKKLTDRAI
KQVPNAIHIS VDNFLNSPRY DELLENLK
