SACX_BACSU
ID SACX_BACSU Reviewed; 459 AA.
AC P15400;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Negative regulator of SacY activity;
DE AltName: Full=PTS system sac EIIBC component;
DE Includes:
DE RecName: Full=Phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system EIIB component;
DE Includes:
DE RecName: Full=Permease IIC component;
DE AltName: Full=PTS system EIIC component;
GN Name=sacX; Synonyms=sacS; OrderedLocusNames=BSU38410; ORFNames=ipa-14r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2116367; DOI=10.1016/0378-1119(90)90453-x;
RA Zukowski M.M., Miller L., Cosgwell P., Chen K., Aymerich S., Steinmetz M.;
RT "Nucleotide sequence of the sacS locus of Bacillus subtilis reveals the
RT presence of two regulatory genes.";
RL Gene 90:153-155(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 348-459.
RC STRAIN=168;
RX PubMed=1806041; DOI=10.3109/10425179109020780;
RA Glaser P., Kunst F., Debarbouille M., Vertes A., Danchin A., Dedonder R.;
RT "A gene encoding a tyrosine tRNA synthetase is located near sacS in
RT Bacillus subtilis.";
RL DNA Seq. 1:251-261(1991).
RN [5]
RP FUNCTION AS A REGULATOR OF SACY.
RX PubMed=11580842; DOI=10.1046/j.1365-2958.2001.02608.x;
RA Tortosa P., Declerck N., Dutartre H., Lindner C., Deutscher J., Le Coq D.;
RT "Sites of positive and negative regulation in the Bacillus subtilis
RT antiterminators LicT and SacY.";
RL Mol. Microbiol. 41:1381-1393(2001).
CC -!- FUNCTION: Negatively regulates SacY activity by catalyzing its
CC phosphorylation on 'His-99'. {ECO:0000269|PubMed:11580842}.
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active -transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system may be involved in sucrose transport.
CC {ECO:0000269|PubMed:11580842}.
CC -!- FUNCTION: Negatively regulates SacY. {ECO:0000269|PubMed:11580842}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The PTS EIIB type-2 domain may serve a regulatory function,
CC through its phosphorylation activity.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; M29333; AAA75335.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51570.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15867.1; -; Genomic_DNA.
DR EMBL; X52480; CAA36719.1; -; Genomic_DNA.
DR PIR; JU0293; JU0293.
DR RefSeq; NP_391720.1; NC_000964.3.
DR RefSeq; WP_003243800.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P15400; -.
DR SMR; P15400; -.
DR STRING; 224308.BSU38410; -.
DR TCDB; 4.A.1.2.10; the pts glucose-glucoside (glc) family.
DR PaxDb; P15400; -.
DR PRIDE; P15400; -.
DR EnsemblBacteria; CAB15867; CAB15867; BSU_38410.
DR GeneID; 937333; -.
DR KEGG; bsu:BSU38410; -.
DR PATRIC; fig|224308.179.peg.4158; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR OMA; QGTFFRY; -.
DR PhylomeDB; P15400; -.
DR BioCyc; BSUB:BSU38410-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0090589; F:protein-phosphocysteine-trehalose phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015771; P:trehalose transport; IBA:GO_Central.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR010973; PTS_IIBC_sucr.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR01996; PTS-II-BC-sucr; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..459
FT /note="Negative regulator of SacY activity"
FT /id="PRO_0000186692"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..86
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 106..459
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 25
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 459 AA; 49024 MW; A5C4E996ECDA3D40 CRC64;
MHKEIAKELL LLAGGKNNII SISHCTTRLR FDVKDETKID IHAIENLQGV QGTFFRYGLF
QIIFGAGVVN KIYKEVVHVW ETAPSEEPVH QKKASRKLNP AAAFAKTLSD IFVPIIPAIT
ASGLLMGLIG MIKVFHWFAA GSPWIKMLDL VSSTAFILLP ILVGFSAARQ FGSNPYLGAV
IAGLLTHPDL LDPSMLGSKT PSSLDIWGLH IPMMGYQGSM IPILLSVFVM SKIEKLLKSI
VPKSLDVVII PFITVMVTGC LALIVMNPAA SIIGQIMTQS IVYIYDHAGI AAGALFGGIY
STIVLSGLHH SFYAIEATLL ANPHVGVNFL VPIWSMANVA QGGAGLAVFL KTKQSSLKKI
ALPASLTAFL GIVEPIVFGV NLKLIRPFIG AAIGGAIGGA YVVAVQVVAN SYGLTGIPMI
SIVLPFGAAN FVHYMIGFLI AAVSAFIATL FLGFKEETE
