LAPA_SHIFL
ID LAPA_SHIFL Reviewed; 102 AA.
AC P0ACV5; P77614;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Lipopolysaccharide assembly protein A {ECO:0000255|HAMAP-Rule:MF_01948};
GN Name=lapA {ECO:0000255|HAMAP-Rule:MF_01948}; Synonyms=yciS;
GN OrderedLocusNames=SF1283, S1366;
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 the assembly of lipopolysaccharide (LPS).
CC {ECO:0000255|HAMAP-Rule:MF_01948}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01948}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01948}.
CC -!- SIMILARITY: Belongs to the LapA family. {ECO:0000255|HAMAP-
CC Rule:MF_01948}.
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DR EMBL; AE005674; AAN42895.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16779.1; -; Genomic_DNA.
DR RefSeq; NP_707188.1; NC_004337.2.
DR RefSeq; WP_000876286.1; NZ_UIQL01000016.1.
DR AlphaFoldDB; P0ACV5; -.
DR STRING; 198214.SF1283; -.
DR EnsemblBacteria; AAN42895; AAN42895; SF1283.
DR EnsemblBacteria; AAP16779; AAP16779; S1366.
DR GeneID; 1026325; -.
DR GeneID; 66674896; -.
DR KEGG; sfl:SF1283; -.
DR KEGG; sfx:S1366; -.
DR PATRIC; fig|198214.7.peg.1504; -.
DR HOGENOM; CLU_160072_0_0_6; -.
DR OMA; QGDYRIS; -.
DR OrthoDB; 2047344at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:InterPro.
DR HAMAP; MF_01948; LPS_assembly_LapA; 1.
DR InterPro; IPR032906; LapA.
DR InterPro; IPR010445; LapA_dom.
DR Pfam; PF06305; LapA_dom; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..102
FT /note="Lipopolysaccharide assembly protein A"
FT /id="PRO_0000168887"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01948"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01948"
FT COILED 64..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01948"
SQ SEQUENCE 102 AA; 11351 MW; 716C2881E2E2EDFC CRC64;
MKYLLIFLLV LAIFVISVTL GAQNDQQVTF NYLLAQGEYR ISTLLAVLFA AGFAIGWLIC
GLFWLRVRVS LARAERKIKR LENQLSPATD VAVVPHSSAA KE
