ID TLPA_BACSU Reviewed; 662 AA.
AC P39216;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Methyl-accepting chemotaxis protein TlpA;
GN Name=tlpA; OrderedLocusNames=BSU31250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / OI1085;
RX PubMed=8188684; DOI=10.1016/s0021-9258(17)36752-2;
RA Hanlon D.W., Ordal G.W.;
RT "Cloning and characterization of genes encoding methyl-accepting chemotaxis
RT proteins in Bacillus subtilis.";
RL J. Biol. Chem. 269:14038-14046(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. All amino acids serve as attractants in B.subtilis, they
CC appear to cause an increase in the turnover methyl groups, leading to
CC methylation of an unidentified acceptor, while repellents have been
CC shown to cause a decrease in methyl group turnover. The methyl groups
CC are added by a methyltransferase and removed by a methylesterase.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; L29189; AAA20555.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15103.1; -; Genomic_DNA.
DR PIR; C54078; C54078.
DR RefSeq; NP_391003.1; NC_000964.3.
DR RefSeq; WP_003243846.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P39216; -.
DR SMR; P39216; -.
DR DIP; DIP-61107N; -.
DR IntAct; P39216; 17.
DR STRING; 224308.BSU31250; -.
DR PaxDb; 224308-BSU31250; -.
DR EnsemblBacteria; CAB15103; CAB15103; BSU_31250.
DR GeneID; 938840; -.
DR KEGG; bsu:BSU31250; -.
DR PATRIC; fig|224308.179.peg.3385; -.
DR eggNOG; COG0840; Bacteria.
DR InParanoid; P39216; -.
DR OrthoDB; 9760371at2; -.
DR PhylomeDB; P39216; -.
DR BioCyc; BSUB:BSU31250-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR PANTHER; PTHR32089:SF114; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00319; TarH; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..662
FT /note="Methyl-accepting chemotaxis protein TlpA"
FT /id="PRO_0000110559"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 152..228
FT /note="Cache"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 374..610
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 370
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 594
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 629
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 636
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 662 AA; 72278 MW; 7335B27992D07FF6 CRC64;
MKKTLTTIRR SSIARRLIIS FLLILIVPIT ALSVSAYQSA VASLDVQMTQ SAKENVQILD
HIIDDKISTT EKSLAYFSDW ATAEKFQDKK KTELKQEFKQ FIQMNDNVAA VFSSGKDGDF
TRYPYADMPS DFNALERDWY KEAMANKGKT IVTEPYESIS SGKMVVTIAR QTVDGSGVVA
IDMKIDDLVT TAKGINIGKE GYAFILSQNK KVIAYSGEKA GTELKGDWVD KLYKDKSGDF
EYTYKGKKKK MAFATSQTTG WKISGTMYAN EIHDAASRVL IMASIVLAIA IGAGMTAIYF
VIRSITKPLR RIVASAEKIS EGDLTETIEI NSKDELGVLS ESFNHMAHSL RSLIHGIKDS
VEHVASSSEE LTASADQTSR ATEHITMAIE QFSNGSESQS EKIETTTEQI NEMNDGLAEL
ARAAAVITET SADSTEVSSK GETLVQKTAG QMNTIDHSVK AAEQVVKGLE IKSKDITNIL
RVINGIADQT NLLALNAAIE AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIESLISEIV
KEIHTSLNVL QSVNKEVETG LVMTDETKQS FKHISQMTNQ IASELQNMNA TVEELSAGAQ
EISAASNDIT AISKESSDGI QDIAASAEEQ LASMEEISSS ALTLERMSEE LRDLTKQFKV
DK
//
