TLPB_BACSU
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 03-AUG-2022, entry version 143.
DE RecName: Full=Methyl-accepting chemotaxis protein TlpB;
GN Name=tlpB; OrderedLocusNames=BSU31230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P39217; -.
DR PRIDE; P39217; -.
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 OMA; YIAHPTI; -.
DR PhylomeDB; P39217; -.
DR BioCyc; BSUB:BSU31230-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 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; SSF103190; SSF103190; 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
