SBMA_ECOLI
ID SBMA_ECOLI Reviewed; 406 AA.
AC P0AFY6; P24212; P71313; P75702; Q2MC48;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Peptide antibiotic transporter SbmA;
GN Name=sbmA; OrderedLocusNames=b0377, JW0368;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Moreno F.;
RL Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=3543211; DOI=10.1099/00221287-132-6-1685;
RA Lavina M., Pugsley A.P., Moreno F.;
RT "Identification, mapping, cloning and characterization of a gene (sbmA)
RT required for microcin B17 action on Escherichia coli K12.";
RL J. Gen. Microbiol. 132:1685-1693(1986).
RN [6]
RP FUNCTION.
RX PubMed=7768835; DOI=10.1128/jb.177.11.3323-3325.1995;
RA Salomon R.A., Farias R.N.;
RT "The peptide antibiotic microcin 25 is imported through the TonB pathway
RT and the SbmA protein.";
RL J. Bacteriol. 177:3323-3325(1995).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17725560; DOI=10.1111/j.1365-2958.2007.05903.x;
RA Mattiuzzo M., Bandiera A., Gennaro R., Benincasa M., Pacor S., Antcheva N.,
RA Scocchi M.;
RT "Role of the Escherichia coli SbmA in the antimicrobial activity of
RT proline-rich peptides.";
RL Mol. Microbiol. 66:151-163(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=26860543; DOI=10.1099/mic.0.000249;
RA Paulsen V.S., Mardirossian M., Blencke H.M., Benincasa M., Runti G.,
RA Nepa M., Haug T., Stensvaag K., Scocchi M.;
RT "Inner membrane proteins YgdD and SbmA are required for the complete
RT susceptibility of Escherichia coli to the proline-rich antimicrobial
RT peptide arasin 1(1-25).";
RL Microbiology 162:601-609(2016).
CC -!- FUNCTION: Uptake of antimicrobial peptides. Required for the transport
CC of microcin B17 (MccB17), microcin 25 (Mcc25) and proline-rich
CC antimicrobial peptides (such as Cathelicidin-3 and Arasin 1) into the
CC cell. {ECO:0000269|PubMed:17725560, ECO:0000269|PubMed:3543211,
CC ECO:0000269|PubMed:7768835, ECO:0000305|PubMed:26860543}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Mutants are resistant to proline-rich
CC antimicrobial peptides of eukaryotic origin.
CC {ECO:0000269|PubMed:17725560, ECO:0000269|PubMed:26860543}.
CC -!- SIMILARITY: Belongs to the peptide uptake permease (PUP) (TC 9.A.18)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18100.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54153; CAA38092.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18100.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73480.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76158.1; -; Genomic_DNA.
DR PIR; A64766; A64766.
DR RefSeq; NP_414911.1; NC_000913.3.
DR RefSeq; WP_001301663.1; NZ_STEB01000007.1.
DR PDB; 7P34; EM; 3.59 A; A/B=1-406.
DR PDBsum; 7P34; -.
DR AlphaFoldDB; P0AFY6; -.
DR SMR; P0AFY6; -.
DR BioGRID; 4259483; 94.
DR STRING; 511145.b0377; -.
DR TCDB; 9.A.18.1.1; the peptide uptake permease (pup) family.
DR jPOST; P0AFY6; -.
DR PaxDb; P0AFY6; -.
DR PRIDE; P0AFY6; -.
DR EnsemblBacteria; AAC73480; AAC73480; b0377.
DR EnsemblBacteria; BAE76158; BAE76158; BAE76158.
DR GeneID; 946884; -.
DR KEGG; ecj:JW0368; -.
DR KEGG; eco:b0377; -.
DR PATRIC; fig|1411691.4.peg.1901; -.
DR EchoBASE; EB0921; -.
DR eggNOG; COG1133; Bacteria.
DR HOGENOM; CLU_045533_0_0_6; -.
DR InParanoid; P0AFY6; -.
DR OMA; TSHYIFR; -.
DR PhylomeDB; P0AFY6; -.
DR BioCyc; EcoCyc:SBMA-MON; -.
DR BioCyc; MetaCyc:SBMA-MON; -.
DR PRO; PR:P0AFY6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015638; F:microcin transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015291; F:secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042885; P:microcin B17 transport; IMP:EcoCyc.
DR GO; GO:0042884; P:microcin transport; IMP:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IDA:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:1901998; P:toxin transport; IDA:EcoCyc.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR009248; SbmA_BacA.
DR Pfam; PF05992; SbmA_BacA; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Peptide transport; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..406
FT /note="Peptide antibiotic transporter SbmA"
FT /id="PRO_0000097603"
FT TOPO_DOM 1..11
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..87
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..205
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..331
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 388
FT /note="S -> T (in Ref. 1; CAA38092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 46459 MW; 684057C831F624CD CRC64;
MFKSFFPKPG TFFLSAFVWA LIAVIFWQAG GGDWVARITG ASGQIPISAA RFWSLDFLIF
YAYYIVCVGL FALFWFIYSP HRWQYWSILG TALIIFVTWF LVEVGVAVNA WYAPFYDLIQ
TALSSPHKVT IEQFYREVGV FLGIALIAVV ISVLNNFFVS HYVFRWRTAM NEYYMANWQQ
LRHIEGAAQR VQEDTMRFAS TLENMGVSFI NAIMTLIAFL PVLVTLSAHV PELPIIGHIP
YGLVIAAIVW SLMGTGLLAV VGIKLPGLEF KNQRVEAAYR KELVYGEDDA TRATPPTVRE
LFSAVRKNYF RLYFHYMYFN IARILYLQVD NVFGLFLLFP SIVAGTITLG LMTQITNVFG
QVRGAFQYLI NSWTTLVELM SIYKRLRSFE HELDGDKIQE VTHTLS
