SUNT_BPSPB
ID SUNT_BPSPB Reviewed; 705 AA.
AC P68580; 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 90.
DE RecName: Full=Sublancin-168-processing and transport ATP-binding protein sunT;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
GN Name=sunT; OrderedLocusNames=SPBc2p021;
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797;
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10376821; DOI=10.1099/13500872-145-5-1055;
RA Lazarevic V., Duesterhoeft A., Soldo B., Hilbert H., Mauel C., Karamata D.;
RT "Nucleotide sequence of the Bacillus subtilis temperate bacteriophage
RT SPbetac2.";
RL Microbiology 145:1055-1067(1999).
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. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. SunT family.
CC {ECO:0000305}.
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DR EMBL; AF020713; AAC12993.1; -; Genomic_DNA.
DR PIR; T12784; T12784.
DR RefSeq; NP_046572.1; NC_001884.1.
DR SMR; P68580; -.
DR MEROPS; C39.A03; -.
DR GeneID; 1261465; -.
DR KEGG; vg:1261465; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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; Host 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="Sublancin-168-processing and transport ATP-binding
FT protein sunT"
FT /id="PRO_0000092982"
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
