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Database: UniProt
Entry: Q5H1Y9_XANOR
LinkDB: Q5H1Y9_XANOR
Original site: Q5H1Y9_XANOR 
ID   Q5H1Y9_XANOR            Unreviewed;       704 AA.
AC   Q5H1Y9;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain {ECO:0000313|EMBL:AAW75032.1};
GN   Name=SunT {ECO:0000313|EMBL:AAW75032.1};
GN   OrderedLocusNames=XOO1778 {ECO:0000313|EMBL:AAW75032.1};
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW75032.1, ECO:0000313|Proteomes:UP000006735};
RN   [1] {ECO:0000313|EMBL:AAW75032.1, ECO:0000313|Proteomes:UP000006735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA   Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA   Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AE013598; AAW75032.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5H1Y9; -.
DR   STRING; 291331.XOO1778; -.
DR   MEROPS; C39.005; -.
DR   KEGG; xoo:XOO1778; -.
DR   PATRIC; fig|291331.8.peg.1978; -.
DR   HOGENOM; CLU_000604_84_3_6; -.
DR   Proteomes; UP000006735; Chromosome.
DR   GO; GO:0005886; C:plasma 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18567; ABC_6TM_CvaB_RaxB_like; 1.
DR   CDD; cd02419; Peptidase_C39C; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR033838; CvaB_peptidase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF606; COLICIN V SECRETION-PROCESSING ATP-BINDING PROTEIN; 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; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006735};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..125
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          159..438
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          471..704
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   704 AA;  77511 MW;  1D7B062CDE6836E9 CRC64;
     MKAIVQAEAS ECGLASLAMV ASAHGMQLDL PELRRRFHLS LKGIRLNQLI EIAQTLGFST
     RPLRLEMEQL DQLSLPCILH WDLNHFVVLA KVGKSKATIL DPAIGERRLS LGEVSQHFTG
     VALELTPTAE FKQHKAAPSI SARQLTGPIR GLWSALSQIA LLSLALQVFV ILAPFYTQWV
     VDQVLVSADR DLLVVLGLGF GLALLLQVGI GLLRGWSVVS LSSRLGLQWM GNVFAHLLKL
     PLDFFEKRHL GDVTSRMSSV QTIQHTLTTS FVEAMIDGVM AMVTLVLMLV YSWKLALVTL
     LAVALYLGIR AIAYRPMRDR TEQQLVAAAK QQTHLLESLR GMQSLKVAGE ESVRRSTYEN
     LLNDTVNQDV KLARMSLGFN TASQLVFGLE RIAVIWIGAR LALDNVFSVG MLVAYLAYKD
     QFAMRVSGLI DKWIEFRMLR LHGERLADIV LTPPEKQHAQ PHALPPAEPS IEVEGLSFRY
     ADGEPWVVKD CSFTIAPGES VAIIGGSGCG KTTLVKLLLG LLTPSEGTIR IGGHDLHKLG
     PRTVRAMIGV VMQDDQLFAG SIADNIGFFD TDFDLERIKA AAQLAAVHED IAAMPMGYHS
     LIGDMGSSLS GGQKQRIILA RALYRQPKLL FLDEATSHLD VTRERLVNEA VKHLQLTKVI
     VAHRPETIAS ADRILVMEHG RIVQEVKLQQ SPEIPHPEDH VLSA
//
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