ARTM_ECOLI
ID ARTM_ECOLI Reviewed; 222 AA.
AC P0AE30; P30862; P77311;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Arginine ABC transporter permease protein ArtM;
GN Name=artM; OrderedLocusNames=b0861, JW0845;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=8501075; DOI=10.1128/jb.175.11.3687-3688.1993;
RA Wissenbach U., Unden G.;
RT "Physical map location of the new artPIQMJ genes of Escherichia coli,
RT encoding a periplasmic arginine transport system.";
RL J. Bacteriol. 175:3687-3688(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8801422; DOI=10.1111/j.1365-2958.1995.mmi_17040675.x;
RA Wissenbach U., Six S., Bongaerts J., Ternes D., Steinwachs S., Unden G.;
RT "A third periplasmic transport system for L-arginine in Escherichia coli:
RT molecular characterization of the artPIQMJ genes, arginine binding and
RT transport.";
RL Mol. Microbiol. 17:675-686(1995).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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. {ECO:0000269|PubMed:8801422}.
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:0000305|PubMed:8801422}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; X86160; CAA60104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73948.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35575.1; -; Genomic_DNA.
DR PIR; E64824; E64824.
DR RefSeq; NP_415382.1; NC_000913.3.
DR RefSeq; WP_000464491.1; NZ_STEB01000019.1.
DR AlphaFoldDB; P0AE30; -.
DR SMR; P0AE30; -.
DR BioGRID; 4263352; 13.
DR BioGRID; 853308; 1.
DR ComplexPortal; CPX-4318; Arginine ABC transporter complex, artI variant.
DR ComplexPortal; CPX-4319; Arginine ABC transporter complex, artJ variant.
DR DIP; DIP-48169N; -.
DR IntAct; P0AE30; 2.
DR STRING; 511145.b0861; -.
DR TCDB; 3.A.1.3.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AE30; -.
DR PaxDb; P0AE30; -.
DR PRIDE; P0AE30; -.
DR EnsemblBacteria; AAC73948; AAC73948; b0861.
DR EnsemblBacteria; BAA35575; BAA35575; BAA35575.
DR GeneID; 66670865; -.
DR GeneID; 949066; -.
DR KEGG; ecj:JW0845; -.
DR KEGG; eco:b0861; -.
DR PATRIC; fig|1411691.4.peg.1416; -.
DR EchoBASE; EB1584; -.
DR eggNOG; COG4160; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR InParanoid; P0AE30; -.
DR OMA; YYILPRQ; -.
DR PhylomeDB; P0AE30; -.
DR BioCyc; EcoCyc:ARTM-MON; -.
DR BioCyc; MetaCyc:ARTM-MON; -.
DR PRO; PR:P0AE30; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IC:ComplexPortal.
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 1: Evidence at protein level;
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_0000059957"
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"
FT CONFLICT 63
FT /note="Q -> R (in Ref. 1; CAA60104)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> V (in Ref. 1; CAA60104)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="L -> V (in Ref. 1; CAA60104)"
FT /evidence="ECO:0000305"
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
