NOSL_PSEST
ID NOSL_PSEST Reviewed; 190 AA.
AC Q52529;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Copper-binding lipoprotein NosL {ECO:0000250|UniProtKB:O68481};
DE Flags: Precursor;
GN Name=nosL {ECO:0000303|PubMed:12618453};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 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: May act as a metallochaperone involved in nitrous oxide
CC reductase assembly. Specifically binds Cu(+).
CC {ECO:0000250|UniProtKB:O68481}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O68481}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303};
CC Periplasmic side {ECO:0000250|UniProtKB:O68481}.
CC -!- INDUCTION: Induced in response to denitrifying conditions. Activation
CC requires NosR and DnrD regulators. {ECO:0000269|PubMed:12618453}.
CC -!- SIMILARITY: Belongs to the NosL family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53676; CAA93438.1; -; Genomic_DNA.
DR PIR; S65468; S65468.
DR RefSeq; WP_003279963.1; NZ_POUM01000011.1.
DR AlphaFoldDB; Q52529; -.
DR SMR; Q52529; -.
DR STRING; 32042.PstZobell_01027; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008719; N2O_reductase_NosL.
DR PANTHER; PTHR41247; PTHR41247; 1.
DR Pfam; PF05573; NosL; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chaperone; Copper; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..190
FT /note="Copper-binding lipoprotein NosL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000439349"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 190 AA; 20443 MW; 3EA6CB6F072661A5 CRC64;
MNALHRIGAG TLLAVLLAFG LTGCGEKEEV QQSLEPVAFH DSDECHVCGM IITDFPGPKG
QAVEKRGVKK FCSTAEMLGW WLQPENRLLD AKLYVHDMGR SVWEKPDDGH LIDATSAYYV
VGTSLKGAMG ASLASFAEEQ DAKALAGMHG GRVLRFEEID QALLQEAASM QHGGMHDHAP
NGAHNAHAGH
