YGAP_ECOLI
ID YGAP_ECOLI Reviewed; 174 AA.
AC P55734; P76625; Q2MAC6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Inner membrane protein YgaP;
GN Name=ygaP; OrderedLocusNames=b2668, JW2643;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-174.
RC STRAIN=K12;
RX PubMed=1480493; DOI=10.1093/nar/20.24.6735;
RA Zhang A., Belfort M.;
RT "Nucleotide sequence of a newly-identified Escherichia coli gene, stpA,
RT encoding an H-NS-like protein.";
RL Nucleic Acids Res. 20:6735-6735(1992).
RN [4]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (JUN-1996).
RN [5]
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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: To Synechocystis PCC 6803 slr1261. {ECO:0000305}.
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DR EMBL; U00096; AAC75715.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76780.1; -; Genomic_DNA.
DR EMBL; X69210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E65046; E65046.
DR RefSeq; NP_417154.1; NC_000913.3.
DR RefSeq; WP_001229442.1; NZ_LN832404.1.
DR PDB; 2MOI; NMR; -; A=2-109.
DR PDB; 2MOL; NMR; -; A=2-109.
DR PDB; 2MPN; NMR; -; A/B=107-174.
DR PDB; 5HBL; X-ray; 1.62 A; A=2-109.
DR PDB; 5HBO; X-ray; 1.66 A; A=2-109.
DR PDB; 5HBP; X-ray; 1.50 A; A=2-109.
DR PDB; 5HBQ; X-ray; 1.66 A; A=2-109.
DR PDB; 5HPA; X-ray; 1.66 A; A=2-109.
DR PDB; 5LAM; NMR; -; A=2-109.
DR PDB; 5LAO; NMR; -; A=2-109.
DR PDBsum; 2MOI; -.
DR PDBsum; 2MOL; -.
DR PDBsum; 2MPN; -.
DR PDBsum; 5HBL; -.
DR PDBsum; 5HBO; -.
DR PDBsum; 5HBP; -.
DR PDBsum; 5HBQ; -.
DR PDBsum; 5HPA; -.
DR PDBsum; 5LAM; -.
DR PDBsum; 5LAO; -.
DR AlphaFoldDB; P55734; -.
DR BMRB; P55734; -.
DR SMR; P55734; -.
DR BioGRID; 4262267; 14.
DR IntAct; P55734; 4.
DR STRING; 511145.b2668; -.
DR jPOST; P55734; -.
DR PaxDb; P55734; -.
DR PRIDE; P55734; -.
DR EnsemblBacteria; AAC75715; AAC75715; b2668.
DR EnsemblBacteria; BAE76780; BAE76780; BAE76780.
DR GeneID; 947135; -.
DR KEGG; ecj:JW2643; -.
DR KEGG; eco:b2668; -.
DR PATRIC; fig|1411691.4.peg.4073; -.
DR EchoBASE; EB3073; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_107126_1_0_6; -.
DR InParanoid; P55734; -.
DR OMA; PRWDLER; -.
DR PhylomeDB; P55734; -.
DR BioCyc; EcoCyc:G7398-MON; -.
DR BioCyc; MetaCyc:G7398-MON; -.
DR PRO; PR:P55734; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:EcoCyc.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR021309; DUF2892.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF11127; DUF2892; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..174
FT /note="Inner membrane protein YgaP"
FT /id="PRO_0000169300"
FT TOPO_DOM 1..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 15..105
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5LAO"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:5HBQ"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5LAO"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:5HBQ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5HBQ"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:5HBQ"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5HBQ"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:5HBQ"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:5HBQ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2MOL"
FT HELIX 116..137
FT /evidence="ECO:0007829|PDB:2MPN"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2MPN"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2MPN"
FT HELIX 146..167
FT /evidence="ECO:0007829|PDB:2MPN"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2MPN"
SQ SEQUENCE 174 AA; 18639 MW; 8B8C923A6F845E1E CRC64;
MALTTISPHD AQELIARGAK LIDIRDADEY LREHIPEADL APLSVLEQSG LPAKLRHEQI
IFHCQAGKRT SNNADKLAAI AAPAEIFLLE DGIDGWKKAG LPVAVNKSQP LPLMRQVQIA
AGGLILIGVV LGYTVNSGFF LLSGFVGAGL LFAGISGFCG MARLLDKMPW NQRA
