ID   A2C5T3_PROM3            Unreviewed;       975 AA.
AC   A2C5T3;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=ABC transporter, multi drug efflux family protein {ECO:0000313|EMBL:ABM76843.1};
GN   OrderedLocusNames=P9303_00861 {ECO:0000313|EMBL:ABM76843.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM76843.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM76843.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM76843.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000554; ABM76843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C5T3; -.
DR   STRING; 59922.P9303_00861; -.
DR   KEGG; pmf:P9303_00861; -.
DR   HOGENOM; CLU_000604_95_0_3; -.
DR   BioCyc; PMAR59922:G1G80-82-MONOMER; -.
DR   Proteomes; UP000002274; 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; 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   SMART; SM00382; AAA; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        418..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        456..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..113
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          274..390
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          420..701
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          736..971
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          229..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   975 AA;  107191 MW;  BFC32AD3620AC3EC CRC64;
     MTLANLNHPL APLQNALQTK GERLKFQIGQ SLCEENYLPG HVLLIESGTA RLLGNRDGRL
     TTRIKLESGS LIGAVSLLRG ESCEAVRAAT ELLAWSITDA TFQQLYNSEK DIRDCCEAYL
     WDAEVAALLQ GIRASTPKSH HSLEAWLKML GPLATLMHAN NDEAEAALNN GKRLFLASSI
     PSCPINTELD SIAAIRELSK PQSGFCLRVI ALPADSLATL LRPAVDSKSN AALQNDEETP
     ETTLSLAPSR PPVSSLNSPS SSEDFFVGGQ GPLQETLACF QMLAKLMKLP FRRDSIEKML
     RDSLRRGQTP TLRMCGQIAA GLGLHVAGAK VPALMGTRLQ TPTLVPWKQS FALVTRSDQL
     GLTLASPSEG FIKLDPSQLE EAFPEGIELL LLDRSNTTPE QAFGPSWFWP ALQRYRGVLI
     QVLIAGFVVQ LFTLANPLLI QVIIDKVINQ RSLDTLQILG FALVIVTVLE GVLGSLKTFL
     FAETTNRIDQ RLGAEVIDHL LRLPLGYFDK RPVGELGSRV SELEKIRNFL TGQALTTLLD
     AAFSVIYVVV MVIYSWLLTL IALAVLPIQV GLTLLGAPLF RRQFRQTAEE NAKTQSHLVE
     VLTGIQTVKA QNVEMISRWK WQERYGRYIS RSFEKTISGT ALSQTSQVLQ KISQLLVLWV
     GASMVLAGDL TLGQLIAFRI ISGYVTQPLL RLSTIWQSIQ ELRVSFERLA DVIDTPQESN
     DLDKGKVPLP PLEGDVSFED LSFSFSKSTA PVLKDISLNI KAGTFVGIVG QSGSGKSTLV
     KLLPRLYSPD QGRILIDGYD IDKVELYSLR RQIGIVPQDP LLFSGSISEN IALTQPDADN
     DEIIMAAKLA VAHDFIMTLP SGYSTPVGER GSSLSGGQRQ RIAIARTLLG NPKLLVMDEA
     TSALDYETER KVCDNLVNAM HDCTVFFITH RLSTVRRADV IVVMHQGAIV EMGTHEALME
     KRGRYYALYR QQESS
//