YBAL_ECOLI
ID YBAL_ECOLI Reviewed; 558 AA.
AC P39830; P52068; P77724; Q2MBU9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Putative cation/proton antiporter YbaL;
GN Name=ybaL; Synonyms=ylaA; OrderedLocusNames=b0478, JW0467;
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;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RC STRAIN=K12 / DH5-alpha;
RA Fujisaki S., Ohnuma S., Horiuchi T., Takahashi I., Tsukui S., Nishimura Y.,
RA Nishino T., Inokuchi H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-558.
RC STRAIN=K12;
RX PubMed=7721718; DOI=10.1128/jb.177.8.2236-2240.1995;
RA Harlow K.W., Nygaard P., Hove-Jensen B.;
RT "Cloning and characterization of the gsk gene encoding guanosine kinase of
RT Escherichia coli.";
RL J. Bacteriol. 177:2236-2240(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND 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).
RN [7] {ECO:0007744|PDB:3FWZ}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 414-550 IN COMPLEX WITH AMP.
RA Chang C., Bigelow L., Buck K., Joachimiak A.;
RT "Crystal structure of TrkA-N domain of inner membrane protein YbaL from
RT Escherichia coli.";
RL Submitted (JAN-2009) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000305}.
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DR EMBL; U82664; AAB40232.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73580.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76257.1; -; Genomic_DNA.
DR EMBL; D73370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L35149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64778; E64778.
DR RefSeq; NP_415011.1; NC_000913.3.
DR RefSeq; WP_000546237.1; NZ_SSZK01000009.1.
DR PDB; 3FWZ; X-ray; 1.79 A; A/B=414-550.
DR PDBsum; 3FWZ; -.
DR AlphaFoldDB; P39830; -.
DR SMR; P39830; -.
DR BioGRID; 4262046; 143.
DR DIP; DIP-11300N; -.
DR IntAct; P39830; 2.
DR STRING; 511145.b0478; -.
DR TCDB; 2.A.37.1.5; the monovalent cation:proton antiporter-2 (cpa2) family.
DR jPOST; P39830; -.
DR PaxDb; P39830; -.
DR PRIDE; P39830; -.
DR EnsemblBacteria; AAC73580; AAC73580; b0478.
DR EnsemblBacteria; BAE76257; BAE76257; BAE76257.
DR GeneID; 946576; -.
DR KEGG; ecj:JW0467; -.
DR KEGG; eco:b0478; -.
DR PATRIC; fig|1411691.4.peg.1798; -.
DR EchoBASE; EB2507; -.
DR eggNOG; COG1226; Bacteria.
DR eggNOG; COG4651; Bacteria.
DR HOGENOM; CLU_005126_9_1_6; -.
DR InParanoid; P39830; -.
DR OMA; TTFSHEG; -.
DR PhylomeDB; P39830; -.
DR BioCyc; EcoCyc:YBAL-MON; -.
DR EvolutionaryTrace; P39830; -.
DR PRO; PR:P39830; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00932; 2a37; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..558
FT /note="Putative cation/proton antiporter YbaL"
FT /id="PRO_0000196616"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..55
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..112
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..185
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..303
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..367
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15919996"
FT DOMAIN 419..541
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT BINDING 427..428
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:3FWZ"
FT BINDING 447..448
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:3FWZ"
FT BINDING 467..468
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:3FWZ"
FT BINDING 494
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:3FWZ"
FT BINDING 514
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:3FWZ"
FT CONFLICT 553..558
FT /note="GEVVTG -> VRW (in Ref. 5; L35149)"
FT /evidence="ECO:0000305"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 427..438
FT /evidence="ECO:0007829|PDB:3FWZ"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:3FWZ"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3FWZ"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 492..505
FT /evidence="ECO:0007829|PDB:3FWZ"
FT STRAND 507..517
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 518..526
FT /evidence="ECO:0007829|PDB:3FWZ"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:3FWZ"
FT HELIX 535..548
FT /evidence="ECO:0007829|PDB:3FWZ"
SQ SEQUENCE 558 AA; 59424 MW; 17DFBAE820B11498 CRC64;
MHHATPLITT IVGGLVLAFI LGMLANKLRI SPLVGYLLAG VLAGPFTPGF VADTKLAPEL
AELGVILLMF GVGLHFSLKD LMAVKAIAIP GAIAQIAVAT LLGMALSAVL GWSLMTGIVF
GLCLSTASTV VLLRALEERQ LIDSQRGQIA IGWLIVEDLV MVLTLVLLPA VAGMMEQGDV
GFATLAVDMG ITIGKVIAFI AIMMLVGRRL VPWIMARSAA TGSRELFTLS VLALALGVAF
GAVELFDVSF ALGAFFAGMV LNESELSHRA AHDTLPLRDA FAVLFFVSVG MLFDPLILIQ
QPLAVLATLA IILFGKSLAA FFLVRLFGHS QRTALTIAAS LAQIGEFAFI LAGLGMALNL
LPQAGQNLVL AGAILSIMLN PVLFALLEKY LAKTETLEEQ TLEEAIEEEK QIPVDICNHA
LLVGYGRVGS LLGEKLLASD IPLVVIETSR TRVDELRERG VRAVLGNAAN EEIMQLAHLE
CAKWLILTIP NGYEAGEIVA SARAKNPDIE IIARAHYDDE VAYITERGAN QVVMGEREIA
RTMLELLETP PAGEVVTG
