ARTM_ECO57
ID ARTM_ECO57 Reviewed; 222 AA.
AC P0AE32; P30862; P77311;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Arginine ABC transporter permease protein ArtM;
GN Name=artM; OrderedLocusNames=Z1091, ECs0944;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in
CC arginine transport. Probably responsible for the translocation of the
CC substrate across the membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ArtP),
CC two transmembrane proteins (ArtM and ArtQ) and two solute-binding
CC proteins (ArtJ and ArtI). {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; AE005174; AAG55240.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34367.1; -; Genomic_DNA.
DR PIR; D85597; D85597.
DR PIR; H90746; H90746.
DR RefSeq; NP_308971.1; NC_002695.1.
DR RefSeq; WP_000464491.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AE32; -.
DR SMR; P0AE32; -.
DR STRING; 155864.EDL933_0994; -.
DR EnsemblBacteria; AAG55240; AAG55240; Z1091.
DR EnsemblBacteria; BAB34367; BAB34367; ECs_0944.
DR GeneID; 66670865; -.
DR GeneID; 917725; -.
DR KEGG; ece:Z1091; -.
DR KEGG; ecs:ECs_0944; -.
DR PATRIC; fig|386585.9.peg.1062; -.
DR eggNOG; COG4160; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR OMA; YYILPRQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
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..222
FT /note="Arginine ABC transporter permease protein ArtM"
FT /id="PRO_0000059958"
FT TOPO_DOM 1..15
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 37..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 71..79
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 101..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 176..186
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 208..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 12..208
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 222 AA; 24914 MW; E9AEF4221C662EDE CRC64;
MFEYLPELMK GLHTSLTLTV ASLIVALILA LIFTIILTLK TPVLVWLVRG YITLFTGTPL
LVQIFLIYYG PGQFPTLQEY PALWHLLSEP WLCALIALSL NSAAYTTQLF YGAIRAIPEG
QWQSCSALGM SKKDTLAILL PYAFKRSLSS YSNEVVLVFK STSLAYTITL MEVMGYSQLL
YGRTYDVMVF GAAGIIYLVV NGLLTLMMRL IERKALAFER RN
