ID   NOSF_PSEST              Reviewed;         308 AA.
AC   P19844;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Probable ABC transporter ATP-binding protein NosF {ECO:0000305};
GN   Name=nosF {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, ATPASE ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, 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). Has ATPase activity
CC       (PubMed:12618453). Could be part of the ABC transporter complex NosDFY
CC       (Probable). {ECO:0000269|PubMed:12618453, ECO:0000269|PubMed:2170125,
CC       ECO:0000305|PubMed:12618453}.
CC   -!- ACTIVITY REGULATION: Inhibited by AMP-PNP. Partially inhibited by N-
CC       ethylmaleimide, orthovanadate and NaN(3).
CC       {ECO:0000269|PubMed:12618453}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3 mM for ATP {ECO:0000269|PubMed:12618453};
CC         KM=10 mM for GTP {ECO:0000269|PubMed:12618453};
CC       pH dependence:
CC         Optimum pH is 8.0-8.5. {ECO:0000269|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       Peripheral membrane protein {ECO:0000305|PubMed:2170125}; Cytoplasmic
CC       side {ECO:0000305|PubMed:2170125}.
CC   -!- INDUCTION: Induced in response to denitrifying conditions. Activation
CC       requires NosR and DnrD regulators. {ECO:0000269|PubMed:12618453}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; X53676; CAA37716.1; -; Genomic_DNA.
DR   PIR; S13584; S13584.
DR   RefSeq; WP_003279967.1; NZ_POUM01000011.1.
DR   PDB; 7O0Y; EM; 3.30 A; B/C=1-308.
DR   PDB; 7O10; EM; 3.60 A; B/C=1-308.
DR   PDB; 7O11; EM; 3.70 A; B/C=1-308.
DR   PDB; 7O12; EM; 3.70 A; B/C=1-308.
DR   PDB; 7O14; EM; -; B/C=1-308.
DR   PDB; 7O15; EM; -; B/C=1-308.
DR   PDB; 7O16; EM; -; B/C=1-308.
DR   PDB; 7O17; EM; 4.50 A; B/C=1-308.
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; P19844; -.
DR   SMR; P19844; -.
DR   STRING; 32042.PstZobell_01037; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW   Membrane; Nucleotide-binding; Transport.
FT   CHAIN           1..308
FT                   /note="Probable ABC transporter ATP-binding protein NosF"
FT                   /id="PRO_0000092645"
FT   DOMAIN          4..228
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   308 AA;  33778 MW;  646A39BC809EF33E CRC64;
     MNAVEIQGVS QRYGSMTVLH DLNLNLGEGE VLGLFGHNGA GKTTSMKLIL GLLSPSEGQV
     KVLGRAPNDP QVRRQLGYLP ENVTFYPQLS GRETLRHFAR LKGAALTQVD ELLEQVGLAH
     AADRRVKTYS KGMRQRLGLA QALLGEPRLL LLDEPTVGLD PIATQDLYLL IDRLRQRGTS
     IILCSHVLPG VEAHINRAAI LAKGCLQAVG SLSQLRAEAG LPVRIRASGI SERDSWLQRW
     TDAGHSARGL SESSIEVVAV NGHKLVLLRQ LLGEGEPEDI EIHQPSLEDL YRYYMERAGD
     VRAQEGRL