ID A3CLV3_STRSV Unreviewed; 526 AA.
AC A3CLV3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=ABC-type multidrug/protein/lipid transport system (Pediocin PA-1 exporter), ATPase and permease components, putative {ECO:0000313|EMBL:ABN44158.1};
GN OrderedLocusNames=SSA_0724 {ECO:0000313|EMBL:ABN44158.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN44158.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN44158.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN44158.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000387; ABN44158.1; -; Genomic_DNA.
DR RefSeq; WP_011836682.1; NC_009009.1.
DR RefSeq; YP_001034708.1; NC_009009.1.
DR AlphaFoldDB; A3CLV3; -.
DR STRING; 388919.SSA_0724; -.
DR KEGG; ssa:SSA_0724; -.
DR PATRIC; fig|388919.9.peg.694; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_9; -.
DR OrthoDB; 95687at2; -.
DR Proteomes; UP000002148; 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 Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 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; 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 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.
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:UP000002148};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..288
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 324..526
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 526 AA; 60244 MW; 69E82FF60F170C52 CRC64;
MLKEILRKYR ASYLGATIFS IGATIFITLF SLQLGVVVDS AQKAHSNLLG QFFICLFCTC
AWSLCSLLAI WFKNNHNKQV LEEVKTRLFH SFYDKNLHDK ASEQENSYLN TTTKNMDIYQ
ENYLTPRCDI VATFSSVFIS TLAIFWIEWR MALGFILISF LTMAASQIPR ILMRKTTANF
TQKSNYFLKQ VTNFLEGFEQ IKLLQIQKRV VEHLSSSNSD FEQARKSYNA AKEGAVTLMM
FFSFLSQIFC MSLGIWFVSQ GSLTIGALIA SVQLLNFVFT PLQLFINNKN LMSTVKDIEN
DFDAKLAKKE AEPAQNLTET IDRIDFEHLG LELGDKALFQ DFSYQFAKDK HYAIIGESGR
GKSTLMKLLL NYFDSKDYAG QIMVNGQAVS QLASDSLYQK ISFIQKNDFF IEGSVADNIA
LYRDINAPDQ TFLYQSLHFN EAFLSKKLDL ERQEVSYGEK QRIDLARFLV KDYDVLIFDE
PTSNLDPSLA AEVMDYILSI KDRIVIVITH NQGRALLDRF DDCLEL
//
