Reviewed, UniProtKB/Swiss-Prot P28008 (PTMCB_STACA)

Names and origin

Protein names

Recommended name:
    PTS system mannitol-specific EIICB component
Alternative name(s):
    EIICB-Mtl
      Short name=EII-Mtl
Including the following 2 domains:
    1- Recommended name:
            Mannitol permease IIC component
        Alternative name(s):
            PTS system mannitol-specific EIIC component
    2- Recommended name:
            Mannitol-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system mannitol-specific EIIB component

Gene names

Name:

mtlA

Organism

Staphylococcus carnosus

Taxonomic identifier

1281 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in mannitol transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subunit structure	Homodimer.
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Induction	By mannitol.
Domain	The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Sequence similarities	Contains 1 PTS EIIB type-2 domain. Contains 1 PTS EIIC type-2 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 518	518	PTS system mannitol-specific EIICB component		PRO_0000186626
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	56 – 76	21	Potential
	Transmembrane	96 – 116	21	Potential
	Transmembrane	142 – 162	21	Potential
	Transmembrane	169 – 189	21	Potential
	Transmembrane	222 – 242	21	Potential
	Transmembrane	276 – 296	21	Potential
	Transmembrane	322 – 342	21	Potential
	Domain	20 – 352	333	PTS EIIC type-2
	Domain	426 – 518	93	PTS EIIB type-2
Sites
	Active site	432	1	Phosphocysteine intermediate Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P28008-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: A0DE0B9E4BA74FA5	FASTA	518	55,686
	10 20 30 40 50 60 MDTMSNSQQN KGIGRKVQAF GSFLSSMIMP NIGAFIAWGF IAAIFIDNGW FPNKDLAQLA 70 80 90 100 110 120 GPMITYLIPL LIAFSGGRLI HDLRGGIIAA TATMGVIVAL PDTPMLLGAM IMGPLVGWLM 130 140 150 160 170 180 KKTDEFVQPR TPQGFEMLFN NFSAGILGFI MTIFGFEVLA PIMKFIMHIL SVGVEALVHA 190 200 210 220 230 240 HLLPLVSILV EPAKIVFLNN AINHGVFTPL GADQAAHAGQ SILYTIESNP GPGIGVLIAY 250 260 270 280 290 300 MIFGKGTAKA TSYGAGIIQF FGGIHEIYFP YVLMRPLLFV SVILGGMTGV ATYSLLDFGF 310 320 330 340 350 360 KTPASPGSII VYAINAPKGE FLHMLTGVVL AALVSFVVSA LILKFTKDPK QDLAEATAQM 370 380 390 400 410 420 EATKGKKSSV ASKLSAKDDN KAADNKTAET TTATAASNKA EDKDSDELLD DYNTEDVDAH 430 440 450 460 470 480 NYNNVDHVIF ACDAGMGSSA MGASMLRNKF KNAGLENIQV TNTAINQLPK NAQLVITQKK 490 500 510 LTDRAIKQSP DAIHISVENF LNSPRYEELI NNLKEDQD

References

[1]	"Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus. Sequence and expression in Escherichia coli and structural comparison with the enzyme IImannitol of Escherichia coli." Fischer R., Hengstenberg W. Eur. J. Biochem. 204:963-969(1992) [PubMed: 1551396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Hengstenberg W. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Expression, purification and characterization of the enzyme II mannitol-specific domain from Staphylococcus carnosus and determination of the active-site cysteine residue." Pogge von Strandmann R., Weigt C., Fischer R., Meyer H.E., Kalbitzer H.R., Hengstenberg W. Eur. J. Biochem. 233:116-122(1995) [PubMed: 7588734] [Abstract] Cited for: ACTIVE SITE CYS-432.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56333 Genomic DNA. Translation: CAA39769.1.
PIR	S22385. S68193.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.69. 3303.
Family and domain databases
InterPro	IPR013011. PTS_EIIB_2. IPR003352. PTS_EIIC. IPR013014. PTS_EIIC_2. IPR003501. PTS_IIB_lac. IPR004718. PTS_IIC_mtl. [Graphical view]
Pfam	PF02378. PTS_EIIC. 1 hit. PF02302. PTS_IIB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00851. mtlA. 1 hit.
PROSITE	PS51099. PTS_EIIB_TYPE_2. 1 hit. PS51104. PTS_EIIC_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTMCB_STACA

Accession

Primary (citable) accession number: P28008

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)