UGPA_SHIFL
ID UGPA_SHIFL Reviewed; 295 AA.
AC Q83PU6; Q7BYU2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=sn-glycerol-3-phosphate transport system permease protein UgpA;
GN Name=ugpA; OrderedLocusNames=SF3470, S4293;
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: Part of the binding-protein-dependent transport system for
CC sn-glycerol-3-phosphate; probably responsible for the translocation of
CC the substrate across the membrane. {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (UgpC),
CC two transmembrane proteins (UgpA and UgpE) and a solute-binding protein
CC (UgpB). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. UgpAE subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN44929.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19253.1; -; Genomic_DNA.
DR RefSeq; NP_709222.1; NC_004337.2.
DR RefSeq; WP_000099287.1; NZ_WPGW01000010.1.
DR AlphaFoldDB; Q83PU6; -.
DR SMR; Q83PU6; -.
DR STRING; 198214.SF3470; -.
DR EnsemblBacteria; AAN44929; AAN44929; SF3470.
DR EnsemblBacteria; AAP19253; AAP19253; S4293.
DR GeneID; 1026473; -.
DR GeneID; 58388342; -.
DR KEGG; sfl:SF3470; -.
DR KEGG; sfx:S4293; -.
DR PATRIC; fig|198214.7.peg.4090; -.
DR HOGENOM; CLU_016047_0_2_6; -.
DR OMA; LWYSVQS; -.
DR OrthoDB; 1688736at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="sn-glycerol-3-phosphate transport system permease
FT protein UgpA"
FT /id="PRO_0000292833"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 33..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 102..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 131..156
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 178..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 229..262
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 284..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 76..284
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 295 AA; 33296 MW; D636CEDE0FB647A9 CRC64;
MSSSRPVFRS RWLPYLLVAP QLIITVIFFI WPAGEALWYS LQSVDPFGFS SQFVGLDNFV
TLFHDSYYLD SFWTTIKFST FVTVSGLLVS LFFAALVEYI VRGSRFYQTL MLLPYAVAPA
VAAVLWIFLF NPGRGLITHF LAEFGYDWNH AQNSGQAMFL VVFASVWKQI SYNFLFFYAA
LQSIPRSLIE AAAIDGAGPI RRFFKIALPL IAPVSFFLLV VNLVYAFFDT FPVIDAATSG
GPVQATTTLI YKIYREGFTG LDLASSAAQS MVLMFLVIVL TVVQFRYVES KVRYQ
