SAPF_SHIFL
ID SAPF_SHIFL Reviewed; 268 AA.
AC P0AAI0; P36637;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Peptide transport system ATP-binding protein SapF;
GN Name=sapF; OrderedLocusNames=SF1295, S1377;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Involved in a peptide intake transport system that plays a
CC role in the resistance to antimicrobial peptides. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN42906.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16789.1; -; Genomic_DNA.
DR RefSeq; NP_707199.1; NC_004337.2.
DR RefSeq; WP_000573407.1; NZ_WPGW01000009.1.
DR AlphaFoldDB; P0AAI0; -.
DR SMR; P0AAI0; -.
DR STRING; 198214.SF1295; -.
DR EnsemblBacteria; AAN42906; AAN42906; SF1295.
DR EnsemblBacteria; AAP16789; AAP16789; S1377.
DR GeneID; 1024268; -.
DR GeneID; 66674883; -.
DR KEGG; sfl:SF1295; -.
DR KEGG; sfx:S1377; -.
DR PATRIC; fig|198214.7.peg.1521; -.
DR HOGENOM; CLU_000604_1_23_6; -.
DR OMA; NPLFTIQ; -.
DR OrthoDB; 1303270at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Peptide transport; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..268
FT /note="Peptide transport system ATP-binding protein SapF"
FT /id="PRO_0000092971"
FT DOMAIN 6..251
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 268 AA; 30571 MW; F3B98BC9DC6DCBFA CRC64;
MIETLLEVRN LSKTFRYRTG WFRRQTVEAV KPLSFTLREG QTLAIIGENG SGKSTLAKML
AGMIEPTSGE LLIDDHPLHF GDYSFRSQRI RMIFQDPSTS LNPRQRISQI LDFPLRLNTD
LEPEQRRKQI IETMRMVGLL PDHVSYYPHM LAPGQKQRLG LARALILRPK VIIADEALAS
LDMSMRSQLI NLMLELQEKQ GISYIYVTQH IGMMKHISDQ VLVMHQGEVV ERGSTADVLA
SPLHELTKRL IAGHFGEALT ADAWRKDR