GLNP_BACSU
ID GLNP_BACSU Reviewed; 218 AA.
AC O34606; Q798Q9;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable glutamine ABC transporter permease protein GlnP;
GN Name=glnP; OrderedLocusNames=BSU27460;
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;
RX PubMed=7551042; DOI=10.1099/13500872-141-7-1781;
RA Rodriguez F., Grandi G.;
RT "An operon encoding a novel ABC-type transport system in Bacillus
RT subtilis.";
RL Microbiology 141:1781-1784(1995).
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).
RN [3]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- FUNCTION: Part of the ABC transporter complex GlnHMPQ involved in
CC glutamine transport. Probably responsible for the translocation of the
CC substrate across the membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GlnQ),
CC two transmembrane proteins (GlnM and GlnP) and a solute-binding protein
CC (GlnH). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; Z69371; CAA93320.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14687.1; -; Genomic_DNA.
DR PIR; F69633; F69633.
DR RefSeq; NP_390623.1; NC_000964.3.
DR RefSeq; WP_003229784.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34606; -.
DR SMR; O34606; -.
DR STRING; 224308.BSU27460; -.
DR PaxDb; O34606; -.
DR EnsemblBacteria; CAB14687; CAB14687; BSU_27460.
DR GeneID; 937556; -.
DR KEGG; bsu:BSU27460; -.
DR PATRIC; fig|224308.179.peg.2982; -.
DR eggNOG; COG0765; Bacteria.
DR InParanoid; O34606; -.
DR OMA; WQSMKLV; -.
DR PhylomeDB; O34606; -.
DR BioCyc; BSUB:BSU27460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..218
FT /note="Probable glutamine ABC transporter permease protein
FT GlnP"
FT /id="PRO_0000376834"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 19..210
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 218 AA; 24165 MW; A6534C99115F743C CRC64;
MDFIGAYSQE HLAFLWDGFL VTLYVAFISI ILSFFFGLIA GTLRYAKVPV LSQLIAVLVE
TIRNLPLLLI IFFTFFALPE IGIKLEITAA AITALTIFES AMLSEIIRSG LKSIDKGQIE
AARSSGLSYT QTLFFIVMPQ ALRRMVPPIV SQFISLLKDT SLAVVIALPE LIHNAQIING
QSADGSYFFP IFLLAALMYF AVNYSLSLAA RRLEVRQT
