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Database: UniProt
Entry: A0A0S2I3L1_9BACT
LinkDB: A0A0S2I3L1_9BACT
Original site: A0A0S2I3L1_9BACT 
ID   A0A0S2I3L1_9BACT        Unreviewed;       726 AA.
AC   A0A0S2I3L1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=RTX-I toxin determinant B {ECO:0000313|EMBL:ALO16810.1};
GN   Name=apxIB_3 {ECO:0000313|EMBL:ALO16810.1};
GN   ORFNames=L21SP5_03195 {ECO:0000313|EMBL:ALO16810.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC   Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16810.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO16810.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16810.1,
RC   ECO:0000313|Proteomes:UP000064893};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of a novel strain predominating
RT   in hypersaline microbial mats and representing a new family of the
RT   Bacteriodetes phylum.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP013118; ALO16810.1; -; Genomic_DNA.
DR   RefSeq; WP_057954159.1; NZ_CP013118.1.
DR   AlphaFoldDB; A0A0S2I3L1; -.
DR   STRING; 1307839.L21SP5_03195; -.
DR   KEGG; blq:L21SP5_03195; -.
DR   PATRIC; fig|1307839.3.peg.3360; -.
DR   OrthoDB; 9760358at2; -.
DR   Proteomes; UP000064893; Chromosome.
DR   GO; GO:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd18571; ABC_6TM_peptidase_like; 1.
DR   CDD; cd02418; Peptidase_C39B; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 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:UP000064893};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..126
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          171..450
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          484..720
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   726 AA;  82742 MW;  6CFFA641E0F7643E CRC64;
     MIFYTQPDAM DCGPTCLRMV AAYYGKHYSL PSLRAKSHIT REGVSLLGIS DAAEAIGFRT
     MGVKVSFDKL KKENPLPCIA HWRENHFVVV YKISGGKVFV ADPGSGKITY TEEEFKQHWA
     KTIVNGELNG ICLLLEPTPT FYETEDEKSN RTKFSFLLKY LRPHRKFLYQ VVLAMLVGSL
     LQLILPFLTQ SVVDVGIANQ DIDFIYLVLI AQMVLFVSQM SVNFIRSWIL LHVSTRINIS
     LISDFLIKLM KLPIGFFDTK MIGDIMQRIG DHRRIEEFLT SQTLSTLFSF INILIFGAVL
     AYYDWTIFWV FVVGTILYIG WILIFMKRRR ELDYKRFQQA SDNQSNLYQL ITGMQEIKLN
     NCEKQKRWDW ERIQAKLFKV SIKGLALSQY QQVGSIFFSE GKNILITVIA ASAVIKGDMT
     LGMMLAVQYI LGQLNNPVSQ LIGFVQSLQD AKISLERLGE IHEKDDEEQP DEPKITMLPE
     KRDIVIENLM FQYEGPHSPK VLEDINLNVF EKKVTAIVGA SGSGKTTLIK LMLGFYEPID
     GNIKLGESQL NNISSRLWRE KCGVVMQDGY IFSDTIANNI AVSDESVDKE KLSHAVKVAN
     IKEFIERLPL GYNTKIGQEG MGISQGQRQR MLIARAVYKN PEFIFFDEAT NALDANNEKV
     IMENLDEFFQ GRTVVVVAHR LSTVKNADQI MVLDKGKMVE LGTHKELVKK KGYYYELVKN
     QLELGN
//
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