NOSY_PSEST
ID NOSY_PSEST Reviewed; 276 AA.
AC P19845;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable ABC transporter permease protein NosY {ECO:0000305};
GN Name=nosY {ECO:0000303|PubMed:2170125};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=2170125; DOI=10.1111/j.1432-1033.1990.tb19265.x;
RA Zumft W.G., Viebrock-Sambale A., Braun C.;
RT "Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for
RT copper-processing and properties of the deduced products, including a new
RT member of the family of ATP/GTP-binding proteins.";
RL Eur. J. Biochem. 192:591-599(1990).
RN [2]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=12618453; DOI=10.1128/jb.185.6.1895-1902.2003;
RA Honisch U., Zumft W.G.;
RT "Operon structure and regulation of the nos gene region of Pseudomonas
RT stutzeri, encoding an ABC-Type ATPase for maturation of nitrous oxide
RT reductase.";
RL J. Bacteriol. 185:1895-1902(2003).
CC -!- FUNCTION: Required for the assembly of the copper chromophores of
CC nitrous oxide reductase (PubMed:2170125). Could be part of the ABC
CC transporter complex NosDFY (Probable). {ECO:0000269|PubMed:2170125,
CC ECO:0000305|PubMed:12618453}.
CC -!- SUBUNIT: The complex may be composed of an ATP-binding protein (NosF),
CC a transmembrane protein (NosY) and a solute-binding protein (NosD).
CC {ECO:0000305|PubMed:12618453}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:2170125};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced in response to denitrifying conditions. Activation
CC requires NosR and DnrD regulators. {ECO:0000269|PubMed:12618453}.
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DR EMBL; X53676; CAA37717.1; -; Genomic_DNA.
DR PIR; S13585; S13585.
DR RefSeq; WP_003279964.1; NZ_POUM01000011.1.
DR PDB; 7O0Y; EM; 3.30 A; D/E=1-276.
DR PDB; 7O10; EM; 3.60 A; D/E=1-276.
DR PDB; 7O11; EM; 3.70 A; D/E=1-276.
DR PDB; 7O12; EM; 3.70 A; D/E=1-276.
DR PDB; 7O14; EM; -; D/E=1-276.
DR PDB; 7O15; EM; -; D/E=1-276.
DR PDB; 7O16; EM; -; D/E=1-276.
DR PDB; 7O17; EM; 4.50 A; D/E=1-276.
DR PDBsum; 7O0Y; -.
DR PDBsum; 7O10; -.
DR PDBsum; 7O11; -.
DR PDBsum; 7O12; -.
DR PDBsum; 7O14; -.
DR PDBsum; 7O15; -.
DR PDBsum; 7O16; -.
DR PDBsum; 7O17; -.
DR AlphaFoldDB; P19845; -.
DR STRING; 32042.PstZobell_01032; -.
DR eggNOG; COG1277; Bacteria.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR InterPro; IPR032688; ABC2_membrane_2.
DR Pfam; PF12679; ABC2_membrane_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..276
FT /note="Probable ABC transporter permease protein NosY"
FT /id="PRO_0000021822"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 276 AA; 29434 MW; 91411E4F00AD8D15 CRC64;
MNQVWNIARK ELSDGLRNRW LLAISLLFAV LAVGIAWLGA AASGQLGFTS IPATIASLAS
LATFLMPLIA LLLAYDAIVG EDEGGTLMLL LTYPLGRGQI LLGKFVGHGL ILALAVLIGF
GCAALAIALL VEGVELGMLF WAFGRFMISS TLLGWVFLAF AYVLSGKVNE KSSAAGLALG
VWFLFVLVFD LVLLALLVLS EGKFNPELLP WLLLLNPTDI YRLINLSGFE GSGSAMGVLS
LGADLPVPAA VLWLCLLAWI GVSLLLAYAI FRRRLT