HISM_SHIFL
ID HISM_SHIFL Reviewed; 238 AA.
AC P0AEU6; P20091; P76936;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Histidine transport system permease protein HisM;
GN Name=hisM; OrderedLocusNames=SF2383, S2518;
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 histidine permease ABC transporter. Also part of
CC a lysine/arginine/ornithine transporter. Probably responsible for the
CC translocation of the substrate across the membrane. Required to relay
CC the ATPase-inducing signal from the solute-binding protein to HisP (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HisP),
CC two transmembrane proteins (HisM and HisQ) and a solute-binding protein
CC (HisJ or ArgT). {ECO:0000250}.
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. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN43896.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17714.1; -; Genomic_DNA.
DR RefSeq; NP_708189.1; NC_004337.2.
DR RefSeq; WP_000569958.1; NZ_WPGN01000023.1.
DR AlphaFoldDB; P0AEU6; -.
DR SMR; P0AEU6; -.
DR STRING; 198214.SF2383; -.
DR EnsemblBacteria; AAN43896; AAN43896; SF2383.
DR EnsemblBacteria; AAP17714; AAP17714; S2518.
DR GeneID; 1025532; -.
DR GeneID; 66673810; -.
DR KEGG; sfl:SF2383; -.
DR KEGG; sfx:S2518; -.
DR PATRIC; fig|198214.7.peg.2850; -.
DR HOGENOM; CLU_019602_1_4_6; -.
DR OMA; KVRYAEF; -.
DR OrthoDB; 1523519at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="Histidine transport system permease protein HisM"
FT /id="PRO_0000060049"
FT TOPO_DOM 1..26
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 48..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 80..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 126..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 179..200
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 222..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..221
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 238 AA; 26870 MW; 0307840A94836348 CRC64;
MIEILHEYWK PLLWTDGYRF TGVAITLWLL ILSVVIGGVL ALFLAIGRVS SNKYIQFPIW
LFTYIFRGTP LYVQLLVFYS GMYTLEIVKG TEFLNAFFRS GLNCTVLALT LNTCAYTTEI
FAGAIRSVPH GEIEAARAYG FSTFKMYRCI ILPSALRIAL PAYSNEVILM LHSTALAFTA
TVPDLLKIAR DINAATYQPF TAFGIAAVLY LIISYVLISL FRRAEKRWLQ HVKPSSTH
