SUNT_BACSU
ID SUNT_BACSU Reviewed; 705 AA.
AC P68579; O30671; O31988; O64034;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=SPbeta prophage-derived sublancin-168-processing and transport ATP-binding protein SunT;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
GN Name=sunT; Synonyms=yolH; OrderedLocusNames=BSU21470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISCUSSION OF FUNCTION.
RC STRAIN=168 / BR151;
RX PubMed=9722542; DOI=10.1074/jbc.273.36.23134;
RA Paik S.H., Chakicherla A., Hansen J.N.;
RT "Identification and characterization of the structural and transporter
RT genes for, and the chemical and biological properties of, sublancin 168, a
RT novel lantibiotic produced by Bacillus subtilis 168.";
RL J. Biol. Chem. 273:23134-23142(1998).
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 REQUIREMENT FOR SUBLANCIN PRODUCTION.
RC STRAIN=168;
RX PubMed=11872755; DOI=10.1074/jbc.m201158200;
RA Dorenbos R., Stein T., Kabel J., Bruand C., Bolhuis A., Bron S., Quax W.J.,
RA Van Dijl J.M.;
RT "Thiol-disulfide oxidoreductases are essential for the production of the
RT lantibiotic sublancin 168.";
RL J. Biol. Chem. 277:16682-16688(2002).
CC -!- FUNCTION: SunT (TC 3.A.1.112.4) is required for production of the
CC lantibiotic sublancin-168, probably by both processing the signal
CC peptide and exporting the resulting mature lantibiotic.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. SunT family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63532.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF014938; AAC63532.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14065.1; -; Genomic_DNA.
DR RefSeq; NP_390030.1; NC_000964.3.
DR RefSeq; WP_003246186.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P68579; -.
DR SMR; P68579; -.
DR STRING; 224308.BSU21470; -.
DR MEROPS; C39.A03; -.
DR TCDB; 3.A.1.112.4; the atp-binding cassette (abc) superfamily.
DR jPOST; P68579; -.
DR PaxDb; P68579; -.
DR PRIDE; P68579; -.
DR EnsemblBacteria; CAB14065; CAB14065; BSU_21470.
DR GeneID; 939124; -.
DR KEGG; bsu:BSU21470; -.
DR PATRIC; fig|224308.179.peg.2344; -.
DR eggNOG; COG2274; Bacteria.
DR eggNOG; COG3271; Bacteria.
DR InParanoid; P68579; -.
DR OMA; DIICTNV; -.
DR PhylomeDB; P68579; -.
DR BioCyc; BSUB:BSU21470-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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; ATP-binding; Bacteriocin transport; Cell membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Protease; Protein transport;
KW Reference proteome; Thiol protease; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..705
FT /note="SPbeta prophage-derived sublancin-168-processing and
FT transport ATP-binding protein SunT"
FT /id="PRO_0000092981"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 306..326
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 TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 12..138
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 168..450
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 483..705
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 516..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 705 AA; 81564 MW; 0F94D9964AF8BD3A CRC64;
MNKKKKYVHT KQFNSHDCGL ACISSILKFH NLNYGIDFLL DLIGDKEGYS LRDLIVIFKK
MGIKTRPLEL QENKTFEALK QIKLPCIALL EGEEYGHYIT IYEIRNNYLL VSDPDKDKIT
KIKKEDFESK FTNFILEIDK ESIPEKEKDQ KKHSYFFKDI LFRNKLIVFV ILLTSLFVVG
LAVAGSFYIK FLVDLIIPRS LRESLITITL IFISMVLIRC IFDFVRSYLI IKLSYKVDKE
MSNVYFNKVT KLPINFFENR EDGEVISRFN DGIYIKDFFS ANFVTAIIDI ILILGLGVIL
YRTNNILFLT IILPILLLSC LAILFFDHLK KKNQKLMEDK AKSTSLLINF LKNMTTVYSL
NKTSFFLEKF HLTYDKQLNS TFSVAKAVIS NEILKGLIQN SFTIIILWVG TRQVLNDSMS
LGTLLFINTL AAFLLSSLDR ILSMQSDLQQ AHVASIRFFD VVNYPVQQDS NENLTELDFI
QNIKTVNLNI GADPMRYIVE DINLILDRKD KVLIIGESGT GKSTFAKSLS KLYKVPDKSI
YLNGLDINRY DHLSIRKRIV YIDENPFLFK GTIKENLCMG EIFDQNEIEN ACIMSQCHEF
ICNLDKQYSY KLSENGSNLS TGQKQRLALA RAILHQPQVL ILDESLSNID PDNTKLIYET
LHRMDCLIIL ITHNDPSNFK YNKKLVFRNN RIIESSYSEN KEYSI
