ASR_SHIFL
ID ASR_SHIFL Reviewed; 102 AA.
AC Q83RD2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Acid shock protein {ECO:0000255|HAMAP-Rule:MF_00546};
DE Flags: Precursor;
GN Name=asr {ECO:0000255|HAMAP-Rule:MF_00546};
GN OrderedLocusNames=SF1618, S1750;
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: Required for growth and/or survival at acidic conditions.
CC {ECO:0000255|HAMAP-Rule:MF_00546}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00546}.
CC -!- PTM: Proteolytic processing gives rise to the active protein.
CC {ECO:0000255|HAMAP-Rule:MF_00546}.
CC -!- SIMILARITY: Belongs to the Asr family. {ECO:0000255|HAMAP-
CC Rule:MF_00546}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN43201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP17089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43201.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17089.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_707494.3; NC_004337.2.
DR AlphaFoldDB; Q83RD2; -.
DR STRING; 198214.SF1618; -.
DR EnsemblBacteria; AAN43201; AAN43201; SF1618.
DR EnsemblBacteria; AAP17089; AAP17089; S1750.
DR GeneID; 1024808; -.
DR KEGG; sfl:SF1618; -.
DR KEGG; sfx:S1750; -.
DR PATRIC; fig|198214.7.peg.1912; -.
DR HOGENOM; CLU_102486_2_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR HAMAP; MF_00546; Asr; 1.
DR InterPro; IPR023497; Acid_shock.
PE 3: Inferred from homology;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT PROPEP 22..58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT /id="PRO_0000269510"
FT CHAIN 59..102
FT /note="Acid shock protein"
FT /id="PRO_0000002409"
FT REGION 22..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 10460 MW; 2C3E5B586D3820AE CRC64;
MKKVLALVVA AAMGLSSAAF AAETATTPAP TATTTKAAPA KTTHHKKQHK AAPAQKAQAA
KKHHKNTKAE QKAPEQKAQA AKKHAGKHGH QQPAKPAAQP AA
