Reviewed, UniProtKB/Swiss-Prot Q9K678 (PTMCB_BACHD)

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
Ordered Locus Names:	BH3854

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannitol transport By similarity.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
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	Kinase Transferase
Technical term	Complete proteome
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-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	PTS system mannitol-specific EIICB component		PRO_0000186608
Regions
	Transmembrane	20 – 40	21	Potential
	Transmembrane	50 – 70	21	Potential
	Transmembrane	93 – 113	21	Potential
	Transmembrane	137 – 157	21	Potential
	Transmembrane	163 – 183	21	Potential
	Transmembrane	215 – 235	21	Potential
	Transmembrane	269 – 289	21	Potential
	Transmembrane	316 – 336	21	Potential
	Domain	14 – 344	331	PTS EIIC type-2
	Domain	380 – 468	89	PTS EIIB type-2
Sites
	Active site	386	1	Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K678-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7B0FDA747E75DEB8	FASTA	468	49,038
	10 20 30 40 50 60 MNNQPSFRAR VQKFGSFLSG MIMPNIGAFI AWGLITALFI PTGWWPNEQL AELVGPMITY 70 80 90 100 110 120 LLPLLIGYTG GKMIYDVRGG VVGAAATMGV VVGADIPMFI GAMIMGPLGG FLIKKVDQVL 130 140 150 160 170 180 QPKVRSGFEM LVNNFSAGIL AAILAIVAFL GIGPVVVSFS NVLASGVEVI IGAGLLPLAS 190 200 210 220 230 240 IFIEPAKVLF LNNAINHGIL SPIGIDQAAS AGKSILFLLE TNPGPGLGVL LAFMVFGKGM 250 260 270 280 290 300 AKQSAPGAAV IHFAGGIHEI YFPYILMKPT LILAVIAGGM SGVFTFVLFN AGLVAVPSPG 310 320 330 340 350 360 SIFALLAMTP RGEYAGVLAG VIIATVVSFV IASIILKTSK ATAEDLTEAT SKMEGLKGKE 370 380 390 400 410 420 SSVKEALITD DEQPQATEVN KIIFACDAGM GSSAMGASIL RDKVKKAGLS IEVANTSINQ 430 440 450 460 LPDDVDIIIT HKDLTDRAKA KNPHAEHISV ENFLSSPKYD ELVNRLKS

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB07573.1.
PIR	F84131.
RefSeq	NP_244721.1.
3D structure databases
SMR	Q9K678. Positions 377-466.
ModBase	Search...
Genome annotation databases
GeneID	892459.
GenomeReviews	Gene locus BH3854 in contig BA000004_GR.
KEGG	bha:BH3854.
NMPDR	fig|272558.1.peg.3854.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG296680.
OMA	GMIMPNI.
PhylomeDB	Q9K678.
Enzyme and pathway databases
BioCyc	BHAL272558:BH3854-MONOMER.
BRENDA	2.7.1.69. 191865.
Family and domain databases
InterPro	IPR013011. PTS_EIIB_2. IPR003501. PTS_EIIB_2/3. IPR003352. PTS_EIIC. IPR013014. PTS_EIIC_2. 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_BACHD

Accession

Primary (citable) accession number: Q9K678

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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