ID   NOSL_ACHCY              Reviewed;         193 AA.
AC   O68481;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Copper-binding lipoprotein NosL {ECO:0000305};
DE   Flags: Precursor;
GN   Name=nosL {ECO:0000303|PubMed:10048486, ECO:0000303|PubMed:9720302};
OS   Achromobacter cycloclastes.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC   102459 / An-17;
RX   PubMed=10048486; DOI=10.1093/dnares/5.6.365;
RA   Inatomi K.;
RT   "Analysis of the nitrous oxide reduction genes, nosZDFYL, of Achromobacter
RT   cycloclastes.";
RL   DNA Res. 5:365-371(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC   102459 / An-17;
RX   PubMed=9720302; DOI=10.1016/s0162-0134(98)10001-6;
RA   McGuirl M.A., Nelson L.K., Bollinger J.A., Chan Y.-K., Dooley D.M.;
RT   "The nos (nitrous oxide reductase) gene cluster from the soil bacterium
RT   Achromobacter cycloclastes: cloning, sequence analysis, and expression.";
RL   J. Inorg. Biochem. 70:155-169(1998).
RN   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11293413; DOI=10.1007/s007750000190;
RA   McGuirl M.A., Bollinger J.A., Cosper N., Scott R.A., Dooley D.M.;
RT   "Expression, purification, and characterization of NosL, a novel Cu(I)
RT   protein of the nitrous oxide reductase (nos) gene cluster.";
RL   J. Biol. Inorg. Chem. 6:189-195(2001).
RN   [4] {ECO:0007744|PDB:2HPU, ECO:0007744|PDB:2HQ3}
RP   STRUCTURE BY NMR OF 21-193.
RX   PubMed=17014077; DOI=10.1021/bi061089+;
RA   Taubner L.M., McGuirl M.A., Dooley D.M., Copie V.;
RT   "Structural studies of Apo NosL, an accessory protein of the nitrous oxide
RT   reductase system: insights from structural homology with MerB, a mercury
RT   resistance protein.";
RL   Biochemistry 45:12240-12252(2006).
CC   -!- FUNCTION: May act as a metallochaperone involved in nitrous oxide
CC       reductase assembly. Specifically binds Cu(+).
CC       {ECO:0000269|PubMed:11293413}.
CC   -!- SUBUNIT: Monomer. Apo-NosL can form homodimers.
CC       {ECO:0000269|PubMed:11293413}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303};
CC       Periplasmic side {ECO:0000269|PubMed:11293413}.
CC   -!- SIMILARITY: Belongs to the NosL family. {ECO:0000305}.
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DR   EMBL; Y15161; CAA75429.1; -; Genomic_DNA.
DR   EMBL; AF047429; AAD09161.1; -; Genomic_DNA.
DR   PDB; 2HPU; NMR; -; A=21-193.
DR   PDB; 2HQ3; NMR; -; A=21-193.
DR   PDBsum; 2HPU; -.
DR   PDBsum; 2HQ3; -.
DR   AlphaFoldDB; O68481; -.
DR   SMR; O68481; -.
DR   EvolutionaryTrace; O68481; -.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chaperone; Copper; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..193
FT                   /note="Copper-binding lipoprotein NosL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5007697109"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          115..124
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           138..147
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:2HPU"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:2HPU"
SQ   SEQUENCE   193 AA;  20449 MW;  463E57C867D25CE8 CRC64;
     MRTRLRFVLV AAALALLSAC KEDVAQSIVP QDMTPETLGH YCQMNLLEHP GPKAQIFLEG
     SPAPLFFSQV RDAIAYARGP EQIAPILVIY VNDMGAAGAT WDQPGDGNWI AADKAFYVVG
     SARRGGMGAP EAVPFSSRDE AAAFVLAEGG QVLALADITD AMVLTPVETG SEPRADDEDY
     LGRLRALPHP AGG