P39214 (MCPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methyl-accepting chemotaxis protein McpA

Alternative name(s):
H1

Gene names

Name:	mcpA
Ordered Locus Names:	BSU31240

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	661 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. McpA is required for taxis towards glucose and alpha-methylglucoside. Ref.1
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Deamidated by CheD on Gln-593 and Gln-594, producing glutamate residues. The glutamate residues are then methylated. Other additional sites are deamidated and methylated as well. Ref.1
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 Direct protein sequencing 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 – 661	661	Methyl-accepting chemotaxis protein McpA		PRO_0000110556
Regions
	Topological domain	1 – 16	16	Cytoplasmic Potential
	Transmembrane	17 – 37	21	Helical; Potential
	Topological domain	38 – 281	244	Extracellular Potential
	Transmembrane	282 – 302	21	Helical; Potential
	Topological domain	303 – 661	359	Cytoplasmic Potential
	Domain	152 – 228	77	Cache
	Domain	303 – 355	53	HAMP
	Domain	374 – 610	237	Methyl-accepting transducer
Amino acid modifications
	Modified residue	370	1	Glutamate methyl ester (Glu) Potential
	Modified residue	593	1	Deamidated glutamine Ref.4
	Modified residue	593	1	Glutamate methyl ester (Gln)
	Modified residue	594	1	Deamidated glutamine Ref.4
	Modified residue	594	1	Glutamate methyl ester (Gln)
	Modified residue	629	1	Glutamate methyl ester (Glu) Potential
	Modified residue	636	1	Glutamate methyl ester (Glu) Potential
Experimental info
	Mutagenesis	593	1	Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-594. Ref.4
	Mutagenesis	594	1	Q → A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-593. Ref.4
	Sequence conflict	95	1	A → R in AAA20556. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39214 [UniParc]. Last modified July 7, 2009. Version 2. Checksum: E46A09AB33604141	FASTA	661	72,314
	10 20 30 40 50 60 MKKILQLIKQ RSITRKLLVS FLSILIIPVV ILAIFAYQSA SSSLDRQMMG SALENVQQLN 70 80 90 100 110 120 EIINTSIGEK ENSADYFSEW LTKEKYNAKS NASIAEKFSQ YISINKDVES IYTSDTKGHF 130 140 150 160 170 180 TRYPDLPMPS GYNPVERDWY KKAVANKGKV VITDPYKTAS TNTMVVTIAQ QTKDGSGVIA 190 200 210 220 230 240 INMTIENLLK TTKKVNIGTQ GYAFIMTKDK KVVAHPNEQS GTELKGDWLD KMLSADKGDF 250 260 270 280 290 300 QYTMDGDKKK MAFDTNKLTG WKIGGTMYLD EIHEAAQPVL HLALIVLAAA IIIGIIVMTL 310 320 330 340 350 360 IIRSITTPLK QLVGSSKRIS EGDLTETIDI RSKDELGELG KSFNNMASSL RSLIHAIQDS 370 380 390 400 410 420 VDNVAASSEE LTASAAQTSK ATEHITLAIE QFSNGNEKQN ENIETAAEHI YQMNDGLTNM 430 440 450 460 470 480 AQASEVITDS SVQSTEIASE GGKLVHQTVG QMNVIDKSVK EAEQVVRGLE TKSKDITNIL 490 500 510 520 530 540 RVINGIADQT NLLALNAAIE AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIIEIV 550 560 570 580 590 600 KEINTSLGMF QSVNQEVQTG LDITDKTEMS FKRISEMTNQ IAGELQNMSA TVQQLSASSE 610 620 630 640 650 660 EVSGASEHIA SISKESSAHI QDIAASAEEQ LASMEEISSS AETLSSMAEE LRDMTKRFKI E

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 95.
[4]	"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: PROTEIN SEQUENCE OF 589-595, DEAMIDATION AT GLN-593 AND GLN-594 BY CHED, MUTAGENESIS OF GLN-593 AND GLN-594.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L29189 Genomic DNA. Translation: AAA20556.1. AL009126 Genomic DNA. Translation: CAB15102.2.
PIR	B54078.
RefSeq	NP_391002.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P39214.
SMR	P39214. Positions 303-355, 364-659.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39214. 23 interactions.
STRING	224308.BSU31240.
Proteomic databases
PaxDb	P39214.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB15102; CAB15102; BSU31240.
GeneID	937154.
KEGG	bsu:BSU31240.
PATRIC	18978206. VBIBacSub10457_3266.
Organism-specific databases
GenoList	BSU31240. [Micado]
Phylogenomic databases
eggNOG	COG0840.
HOGENOM	HOG000083278.
KO	K03406.
ProtClustDB	CLSK2301479.
Enzyme and pathway databases
BioCyc	BSUB:BSU31240-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

MCPA_BACSU

Accession

Primary (citable) accession number: P39214

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