GANP_BACSU
ID GANP_BACSU Reviewed; 418 AA.
AC O32261; O07010;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Galactooligosaccharides transport system permease protein GanP {ECO:0000305};
GN Name=ganP; Synonyms=yvfL; OrderedLocusNames=BSU34150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 PUTATIVE FUNCTION.
RX PubMed=17056685; DOI=10.1128/aem.01306-06;
RA Shipkowski S., Brenchley J.E.;
RT "Bioinformatic, genetic, and biochemical evidence that some glycoside
RT hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer
RT hydrolases.";
RL Appl. Environ. Microbiol. 72:7730-7738(2006).
RN [4]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RX PubMed=27501980; DOI=10.1128/jb.00468-16;
RA Watzlawick H., Morabbi Heravi K., Altenbuchner J.;
RT "Role of the ganSPQAB operon in degradation of galactan by Bacillus
RT subtilis.";
RL J. Bacteriol. 198:2887-2896(2016).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=29240795; DOI=10.1371/journal.pone.0189483;
RA Ferreira M.J., Mendes A.L., de Sa-Nogueira I.;
RT "The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus
RT subtilis.";
RL PLoS ONE 12:e0189483-e0189483(2017).
CC -!- FUNCTION: Involved in galactan degradation (PubMed:27501980). Part of
CC the ABC transporter complex GanPQS involved in the uptake of
CC galactooligosaccharides (PubMed:27501980, PubMed:29240795). Responsible
CC for the translocation of the substrate across the membrane (Probable).
CC {ECO:0000269|PubMed:27501980, ECO:0000269|PubMed:29240795, ECO:0000305,
CC ECO:0000305|PubMed:17056685}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC two transmembrane proteins (GanP and GanQ) and a solute-binding protein
CC (GanS). {ECO:0000269|PubMed:27501980, ECO:0000269|PubMed:29240795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Repressed by the transcriptional regulator GanR and induced
CC by galactobiose. Also repressed by glucose.
CC {ECO:0000269|PubMed:27501980}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB08006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z94043; CAB08006.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15420.1; -; Genomic_DNA.
DR PIR; D70038; D70038.
DR RefSeq; NP_391295.1; NC_000964.3.
DR RefSeq; WP_003243623.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32261; -.
DR SMR; O32261; -.
DR STRING; 224308.BSU34150; -.
DR TCDB; 3.A.1.1.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; O32261; -.
DR PRIDE; O32261; -.
DR EnsemblBacteria; CAB15420; CAB15420; BSU_34150.
DR GeneID; 936323; -.
DR KEGG; bsu:BSU34150; -.
DR PATRIC; fig|224308.179.peg.3702; -.
DR eggNOG; COG1175; Bacteria.
DR InParanoid; O32261; -.
DR OMA; QYIYQMA; -.
DR PhylomeDB; O32261; -.
DR BioCyc; BSUB:BSU34150-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:1990060; C:maltose transport complex; IBA:GO_Central.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..418
FT /note="Galactooligosaccharides transport system permease
FT protein GanP"
FT /id="PRO_0000382424"
FT TRANSMEM 25..45
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 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 187..407
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 418 AA; 46978 MW; 0B4220314DDD6A66 CRC64;
MQHRQVALLL SIIPGLGQFY NKQWIKGIVF LFLGASFFAV FGDLLNMGFW GIFTLGTEVP
RDNSVFLLAE GIIAVIVTCF GLAVYYVNLR DAFQSGKQRD ENKPLSSLKE QYQHIISEGY
PYVVSGPSLF ILIFAVIFPI LFSFALAFTN YDLYHSPPAK LIDWVGFQTF ANIFTVDIWR
STFFDVLAWT VVWTLAASTL QVTLGIFLAI IVNQKDLRFK RFFRTILILP WAVPGFVTIL
IFAGLFNDSF GAMNHDILAF FGIDPLPWMT DANWSRLALI LMQGWLGFPY IFLVSTGVLQ
SIPDDLYEAA TIDGASVFSK LRYITLPMVF IAMAPIIITQ FTFNFNNFNI IYLFNGGGPA
VTGSTAGGTD ILVSWIYKLT MQSSQYSLAA ALTILLSVFV ISIALWQFRQ TKSFKEEA
