ID NOSF_STUST Reviewed; 308 AA.
AC P19844;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Probable ABC transporter ATP-binding protein NosF {ECO:0000305};
GN Name=nosF {ECO:0000303|PubMed:2170125};
OS Stutzerimonas stutzeri (Pseudomonas stutzeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Stutzerimonas.
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 / Baumann 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 / Baumann 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; 7O0Z; EM; 3.70 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; 7O13; EM; 3.60 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 PDB; 7OSF; EM; 3.80 A; B/C=1-308.
DR PDB; 7OSG; EM; 3.30 A; B/C=1-308.
DR PDB; 7OSH; EM; 3.80 A; B/C=1-308.
DR PDB; 7OSI; EM; 3.80 A; B/C=1-308.
DR PDB; 7OSJ; EM; 3.80 A; B/C=1-308.
DR PDB; 7QBA; EM; 3.78 A; B/C=2-308.
DR PDB; 7ZNQ; EM; 3.04 A; F/f=1-308.
DR PDBsum; 7O0Y; -.
DR PDBsum; 7O0Z; -.
DR PDBsum; 7O10; -.
DR PDBsum; 7O11; -.
DR PDBsum; 7O12; -.
DR PDBsum; 7O13; -.
DR PDBsum; 7O14; -.
DR PDBsum; 7O15; -.
DR PDBsum; 7O16; -.
DR PDBsum; 7O17; -.
DR PDBsum; 7OSF; -.
DR PDBsum; 7OSG; -.
DR PDBsum; 7OSH; -.
DR PDBsum; 7OSI; -.
DR PDBsum; 7OSJ; -.
DR PDBsum; 7QBA; -.
DR PDBsum; 7ZNQ; -.
DR AlphaFoldDB; P19844; -.
DR EMDB; EMD-12683; -.
DR EMDB; EMD-12684; -.
DR EMDB; EMD-12685; -.
DR EMDB; EMD-12686; -.
DR EMDB; EMD-12687; -.
DR EMDB; EMD-12688; -.
DR EMDB; EMD-12689; -.
DR EMDB; EMD-12690; -.
DR EMDB; EMD-12691; -.
DR EMDB; EMD-12692; -.
DR EMDB; EMD-13049; -.
DR EMDB; EMD-13050; -.
DR EMDB; EMD-13051; -.
DR EMDB; EMD-13052; -.
DR EMDB; EMD-13053; -.
DR EMDB; EMD-13885; -.
DR EMDB; EMD-14813; -.
DR SMR; P19844; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03230; ABC_DR_subfamily_A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR42939; ABC TRANSPORTER ATP-BINDING PROTEIN ALBC-RELATED; 1.
DR PANTHER; PTHR42939:SF1; ABC TRANSPORTER ATP-BINDING PROTEIN ALBC-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:7OSG"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:7O14"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:7O0Y"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:7OSG"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:7ZNQ"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:7ZNQ"
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
//
