ID   TLPB_BACSU              Reviewed;         662 AA.
AC   P39217;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Methyl-accepting chemotaxis protein TlpB;
GN   Name=tlpB; OrderedLocusNames=BSU31230;
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; AAA20557.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15101.1; -; Genomic_DNA.
DR   PIR; D54078; D54078.
DR   RefSeq; NP_391001.1; NC_000964.3.
DR   RefSeq; WP_003243983.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P39217; -.
DR   SMR; P39217; -.
DR   STRING; 224308.BSU31230; -.
DR   jPOST; P39217; -.
DR   PaxDb; 224308-BSU31230; -.
DR   EnsemblBacteria; CAB15101; CAB15101; BSU_31230.
DR   GeneID; 937152; -.
DR   KEGG; bsu:BSU31230; -.
DR   PATRIC; fig|224308.179.peg.3383; -.
DR   eggNOG; COG0840; Bacteria.
DR   InParanoid; P39217; -.
DR   OrthoDB; 9760371at2; -.
DR   PhylomeDB; P39217; -.
DR   BioCyc; BSUB:BSU31230-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; 6.10.340.10; -; 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 TlpB"
FT                   /id="PRO_0000110560"
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          153..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 (Gln)"
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;  71536 MW;  91215F86293D7425 CRC64;
     MGKFIQWIKQ PSISKPLIAA FLAVLILPVG VLAYFSYQSA WNALDRELIS SAKGNVEELN
     STLQNKLEDK VKAIDYYSET VDKDILLGKN KTLLKEKFKQ YTTLNDDVGA IYAASEDKKL
     YKYPDSGVPK GFDPTGRDWY KQAVAEKGQA VFSEPYTDEA TGDIVVTISK QLKDGSGVIA
     LDLNLDEVLT ASKRIKIGKE GFAFITTGNK KYIAHPTIKP GTTGSGDWTN QVYSKKEGSF
     EYTFEGKEKK MAFTTNKLTG WKIAGTYFVS ELQDASSPVL NTAVIILCVS IVIGGILILY
     IIRAITKPLR KLVSTSAKIS SGDLTEVIDI HSKNEFGQLG ESFNEMSASL RSVIGVIQTS
     VENVASSSEE LTASAAQTSK ATEHITLAIE QFSDGNEAQS EKLETSSNHL SQMNEGISKV
     AQASSTITKS SIQSSEAAGS GEKLVEHTVG QMKTIDQSVQ KAEAVVKGLE TKSQDITSIL
     NVINGIADQT NLLALNAAIE AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIQEIV
     REISTSLSMF QSVNHEVKEG LQITDQTAES FKQIYEMTTQ ISGELQNLNA TVEQLSAGSQ
     EVSSAVEDIS AVAKESSAGI QDIAASAEEQ LASMEEISSS AETLANMAEE LQDITKKFKI
     ES
//