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Database: UniProt
Entry: A0A1Y0RJ94_9CYAN
LinkDB: A0A1Y0RJ94_9CYAN
Original site: A0A1Y0RJ94_9CYAN 
ID   A0A1Y0RJ94_9CYAN        Unreviewed;       992 AA.
AC   A0A1Y0RJ94;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Type I secretion system permease/ATPase {ECO:0000313|EMBL:ARV60083.1};
GN   ORFNames=BZZ01_16945 {ECO:0000313|EMBL:ARV60083.1};
OS   Nostocales cyanobacterium HT-58-2.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX   NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV60083.1, ECO:0000313|Proteomes:UP000196302};
RN   [1] {ECO:0000313|EMBL:ARV60083.1, ECO:0000313|Proteomes:UP000196302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV60083.1,
RC   ECO:0000313|Proteomes:UP000196302};
RA   Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT   "Genome sequences and microbial community composition of HT-58-2, a
RT   tolyporphin-producing cyanobacterium-microbial holobiont.";
RL   Submitted (FEB-2017) 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; CP019636; ARV60083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0RJ94; -.
DR   KEGG; ncn:BZZ01_16945; -.
DR   OrthoDB; 516912at2; -.
DR   Proteomes; UP000196302; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18782; ABC_6TM_PrtD_LapB_HlyB_like; 1.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd02259; Peptidase_C39_like; 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; 2.60.120.10; Jelly Rolls; 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; IPR010132; ATPase_T1SS_HlyB.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR01846; type_I_sec_HlyB; 1.
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; PF00027; cNMP_binding; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 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; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        435..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        546..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        573..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..119
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          285..407
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          439..718
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          752..987
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   992 AA;  111552 MW;  0BB52B32B6741FCF CRC64;
     MTYTASIQEF ISELFPFNQL PSLELAKLIS KFEMLRYRMG QSVLVREQMP AQISIIYEGQ
     ARLLSYDPNT QMPETLQLVK KGEILGWISL LRGSPCETVI ASTETVCLTL PATEFLALLR
     NSPAVGICFE NRCSAIEVFE LLSTELGKRA DSDAVLASYG ATDIKELTLK VLDEAVVCTF
     LEERIPLEQL DPELVWFVSG GILKDFPVGS RLQLDDVVTY LEVQSFGYVR LVGLPRTTLS
     ASASAVRDPF RINPLLEQIP YAPDHPLQLE KPSDKKSRPK YPHVRGRGPI NATLACFQML
     SQHLNMPFRR DVILQILNNQ VERTQTLSLQ LCGAIAELVG LNTQLVDVSA KAITKLQAPA
     MIRWQDTFAI LFEISEKKLV LGVPEVGIVH QEPDYFVENW GEEGQVLLLK LAKYTPRQRF
     SLRWFLPSLL QYRKVLLEVL IASFFVQVFS LANPLVIQVI IDKVIIQNGF ETLNVLGVLL
     LIMAVFEGLL TSVRTYLFVD TTNRIDLALG SEIIDRLFRL PLRYFERRPV GELATRANEL
     ENIRSFMTGT ALTVVLDAVF SAIYIVVMLV YSWMLTLVAL LTVPVFAFVT MIFSSIMRRQ
     LRFKAERYSE TQSYLVEALS GIQTVKAQNI ELRSRWQWQQ HYSKYVTAGF QTVVTSTAAS
     VTSNFLNQVS SLSVLWVGAY LVLQGQLSLG QLIAFRIIAG YVTAPLLRLT QLWQNFQETA
     LSLERLADIL DTPSEIDEDR DNITLPPVKG AVKYENVSFR FTPSGPLQLN NINLDFPPGK
     FVGIVGQSGS GKSTLTKLLP RLYDLESGRI LVDGYDISKI ELYSLRRQIG MVLQDSLLFD
     GTIRENIALT NPDATADEII EAAEIAAAHE FIMSLPNGYN TRVGERGSAL SGGQRQRIAI
     ARTVLQNPRL LILDEATSAL DYQSERQVCQ NLAQAFRDRT VFFITHRLST VKNADIILLL
     DRGIVVEQGT HDELMVQQGR YYCLFQQQEA QL
//
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