POTI_ECOLI
ID POTI_ECOLI Reviewed; 281 AA.
AC P0AFL1; P31136;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putrescine transport system permease protein PotI {ECO:0000305};
GN Name=potI {ECO:0000303|PubMed:8416922}; OrderedLocusNames=b0857, JW0841;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=8416922; DOI=10.1016/s0021-9258(18)54126-0;
RA Pistocchi R., Kashiwagi K., Miyamoto S., Nukui E., Sadakata Y.,
RA Kobayashi H., Igarashi K.;
RT "Characteristics of the operon for a putrescine transport system that maps
RT at 19 minutes on the Escherichia coli chromosome.";
RL J. Biol. Chem. 268:146-152(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 SUBCELLULAR LOCATION.
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).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=23719730; DOI=10.1007/s00726-013-1517-x;
RA Terui Y., Saroj S.D., Sakamoto A., Yoshida T., Higashi K., Kurihara S.,
RA Suzuki H., Toida T., Kashiwagi K., Igarashi K.;
RT "Properties of putrescine uptake by PotFGHI and PuuP and their
RT physiological significance in Escherichia coli.";
RL Amino Acids 46:661-670(2014).
CC -!- FUNCTION: Part of the ABC transporter complex PotFGHI involved in
CC putrescine uptake (PubMed:8416922, PubMed:23719730). Responsible for
CC the translocation of the substrate across the membrane (Probable).
CC Imports putrescine for maintenance of the optimal concentration of
CC polyamines necessary for cell growth in the presence of glucose
CC (PubMed:23719730). {ECO:0000269|PubMed:23719730,
CC ECO:0000269|PubMed:8416922, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Transport is feedback inhibited by intracellular
CC polyamines. {ECO:0000269|PubMed:23719730}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PotG),
CC two transmembrane proteins (PotH and PotI) and a solute-binding protein
CC (PotF). {ECO:0000269|PubMed:23719730, ECO:0000269|PubMed:8416922}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; M93239; AAA24412.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73944.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35568.1; -; Genomic_DNA.
DR PIR; D45313; D45313.
DR RefSeq; NP_415378.1; NC_000913.3.
DR RefSeq; WP_001061658.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P0AFL1; -.
DR SMR; P0AFL1; -.
DR BioGRID; 4259996; 3.
DR ComplexPortal; CPX-4384; Putrescine ABC transporter complex.
DR STRING; 511145.b0857; -.
DR TCDB; 3.A.1.11.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AFL1; -.
DR PRIDE; P0AFL1; -.
DR EnsemblBacteria; AAC73944; AAC73944; b0857.
DR EnsemblBacteria; BAA35568; BAA35568; BAA35568.
DR GeneID; 67413899; -.
DR GeneID; 945485; -.
DR KEGG; ecj:JW0841; -.
DR KEGG; eco:b0857; -.
DR PATRIC; fig|1411691.4.peg.1420; -.
DR EchoBASE; EB1589; -.
DR eggNOG; COG1177; Bacteria.
DR HOGENOM; CLU_016047_3_0_6; -.
DR InParanoid; P0AFL1; -.
DR OMA; FPMFVWG; -.
DR PhylomeDB; P0AFL1; -.
DR BioCyc; EcoCyc:POTI-MON; -.
DR BioCyc; MetaCyc:POTI-MON; -.
DR PRO; PR:P0AFL1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:EcoCyc.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..281
FT /note="Putrescine transport system permease protein PotI"
FT /id="PRO_0000060189"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..33
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 34..68
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 89..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 136..140
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 161..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 207..243
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 264..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..260
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 281 AA; 30541 MW; A1B557CE2FC7C9EB CRC64;
MNNLPVVRSP WRIVILLLGF TFLYAPMLML VIYSFNSSKL VTVWAGWSTR WYGELLRDDA
MMSAVGLSLT IAACAATAAA ILGTIAAVVL VRFGRFRGSN GFAFMITAPL VMPDVITGLS
LLLLFVALAH AIGWPADRGM LTIWLAHVTF CTAYVAVVIS SRLRELDRSI EEAAMDLGAT
PLKVFFVITL PMIMPAIISG WLLAFTLSLD DLVIASFVSG PGATTLPMLV FSSVRMGVNP
EINALATLIL GAVGIVGFIA WYLMARAEKQ RIRDIQRARR G
