P39215 (MCPB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methyl-accepting chemotaxis protein McpB

Alternative name(s):
H3

Gene names

Name:	mcpB
Ordered Locus Names:	BSU31260

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpB is required for taxis towards asparagine, aspartate, glutamine, and histidine. Ref.1
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated. Ref.1 Ref.4 The demethylation is selective. Gln-371 is demethylated only upon asparagine addition whereas Glu-637 is demethylated only upon asparagine removal. Glu-630 appears indiscriminate and is demethylated upon both addition and removal of asparagine. Ref.1 Ref.4
Miscellaneous	Only chemotaxis towards asparagine is completely deficient in the absence of McpB.
Sequence similarities	Contains 1 cache domain. Contains 1 HAMP domain. Contains 1 methyl-accepting transducer domain.

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transducer
PTM	Methylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis 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	transmembrane signaling receptor 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 – 662	662	Methyl-accepting chemotaxis protein McpB		PRO_0000110557
Regions
	Topological domain	1 – 16	16	Cytoplasmic Potential
	Transmembrane	17 – 37	21	Helical; Potential
	Topological domain	38 – 282	245	Extracellular Potential
	Transmembrane	283 – 303	21	Helical; Potential
	Topological domain	304 – 662	359	Cytoplasmic Potential
	Domain	153 – 229	77	Cache
	Domain	304 – 356	53	HAMP
	Domain	375 – 611	237	Methyl-accepting transducer
Amino acid modifications
	Modified residue	371	1	Glutamate methyl ester (Gln) Ref.4
	Modified residue	630	1	Glutamate methyl ester (Glu) Ref.4
	Modified residue	637	1	Glutamate methyl ester (Glu) Ref.4
Experimental info
	Mutagenesis	371	1	Q → D: Marked diminution of methanol upon both addition and removal of asparagine. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-630. Release of methanol upon both asparagine addition and removal; when associated with D-637. No methylation; when associated with D-630 and D-637. Ref.4
	Mutagenesis	595	1	Q → D: Wild-type production of methanol. Ref.4
	Mutagenesis	630	1	E → D: Marked diminution of methanol upon both addition and removal of asparagine; methanol release delayed by about 1 minute compared to wild-type; adapts normally to addition of asparagine but fails to adapt to asparagine removal. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-637. No methylation; when associated with D-371 and D-637. Ref.4
	Mutagenesis	637	1	E → D: Marked diminution of methanol upon both addition and removal of asparagine; fails to adapt to addition of asparagine. Release of methanol upon both asparagine addition and removal; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-630. No methylation; when associated with D-371 and D-630. Ref.4
	Sequence conflict	360	1	D → N in AAA20554. Ref.1
	Sequence conflict	402	1	E → R in AAA20554. Ref.1
	Sequence conflict	450	1	V → G in AAA20554. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39215 [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 2E4ED0EFC31F2983	FASTA	662	71,901
	10 20 30 40 50 60 MKTFINWLKK PSISKKLIVS FIAILIIPIL ILEFSSYRSA SGKLDQEIMG NAKNSVDTFN 70 80 90 100 110 120 TTVTNDLGEK AKAVTFFSES LKRSAFKGKS NQEEIKAKFS QYVSINQGVA RIYGGADNGT 130 140 150 160 170 180 YVQAPKEKLP EGYDPRQRPW YQDAMKAGGE IVVTDPYVAA SDGSMVITIA QELKDGSGVV 190 200 210 220 230 240 AMDITIDKLL EQMKQIKVGK EGYAFIATKN KTYVAHKNHK AGEKLSGDWV AKMYANDSGE 250 260 270 280 290 300 LQYTLNNEDK KMTYTTNELT GWKIAGTMYM DEIKDASKSV LTTGMIVLIA SIVAGGILIL 310 320 330 340 350 360 FIVRSITKPL KRLVQSSKTI SRGDLTETIE IHSKDELGEL GESFNEMGQS LRSLISAIQD 370 380 390 400 410 420 SVNNVAASSE QLTASAGQTS KATEHITMAI EQFSNGNEEQ SEKVESSSHQ LNLMNEGLQQ 430 440 450 460 470 480 VSQTSSDITK ASIQSTEIAG TGEKFVQQTV GQMNSINQSV QQAEAVVKGL EGKSKDITSI 490 500 510 520 530 540 LRVINGIADQ TNLLALNAAI EAARAGESGR GFSVVAEEVR KLAVQSADSA KEIEKLIQEI 550 560 570 580 590 600 VAEIDTSLHM FKEVNQEVQS GLVVTDNTKE SFQSIFSMTN EIAGKLQTMN STVEQLSDRS 610 620 630 640 650 660 QHVSAAVSGI ADVSKESSAS IQDIAASAEE QLASMEEISS SATTLAQMAE ELRDLTKQFK IE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis." Hanlon D.W., Ordal G.W. J. Biol. Chem. 269:14038-14046(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POTENTIAL METHYLATION SITES, FUNCTION. Strain: 168 / OI1085.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 360; 402 AND 450.
[4]	"Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation." Zimmer M.A., Tiu J., Collins M.A., Ordal G.W. J. Biol. Chem. 275:24264-24272(2000) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT GLN-371; GLU-630 AND GLU-637, MUTAGENESIS OF GLN-371; GLN-595; GLU-630 AND GLU-637.
[5]	"Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis." Kristich C.J., Ordal G.W. J. Biol. Chem. 277:25356-25362(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DEAMIDATION BY CHED.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L29189 Genomic DNA. Translation: AAA20554.1. AL009126 Genomic DNA. Translation: CAB15104.2.
PIR	A54078.
RefSeq	NP_391004.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P39215.
SMR	P39215. Positions 304-356, 360-660.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39215. 2 interactions.
STRING	224308.BSU31260.
Proteomic databases
PaxDb	P39215.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB15104; CAB15104; BSU31260.
GeneID	937155.
KEGG	bsu:BSU31260.
PATRIC	18978210. VBIBacSub10457_3268.
Organism-specific databases
GenoList	BSU31260. [Micado]
Phylogenomic databases
eggNOG	COG0840.
HOGENOM	HOG000083278.
KO	K03406.
ProtClustDB	CLSK2301479.
Enzyme and pathway databases
BioCyc	BSUB:BSU31260-MONOMER.
Family and domain databases
InterPro	IPR004010. Cache_domain. IPR003122. Chemotax_Me-accpt_rcpt_lig-bd. IPR003660. HAMP_linker_domain. IPR004089. MCPsignal_dom. [Graphical view]
Pfam	PF02743. Cache_1. 1 hit. PF00672. HAMP. 1 hit. PF00015. MCPsignal. 1 hit. PF02203. TarH. 1 hit. [Graphical view]
SMART	SM00304. HAMP. 1 hit. SM00283. MA. 1 hit. SM00319. TarH. 1 hit. [Graphical view]
PROSITE	PS00538. CHEMOTAXIS_TRANSDUC_1. False negative. PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit. PS50885. HAMP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCPB_BACSU

Accession

Primary (citable) accession number: P39215

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program