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
//