AUPA_MARN1
ID AUPA_MARN1 Reviewed; 452 AA.
AC H8WEC1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Alkane uptake protein A {ECO:0000303|PubMed:29871914};
DE Flags: Precursor;
GN Name=aupA {ECO:0000303|PubMed:29871914};
GN ORFNames=MARHY0478 {ECO:0000312|EMBL:CCG93977.1};
OS Marinobacter nauticus (strain ATCC 49840 / DSM 8798 / CIP 103578 / SP17)
OS (Marinobacter hydrocarbonoclasticus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=1163748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49840 / DSM 8798 / CIP 103578 / SP17;
RX PubMed=22689231; DOI=10.1128/jb.00500-12;
RA Grimaud R., Ghiglione J.F., Cagnon C., Lauga B., Vaysse P.J.,
RA Rodriguez-Blanco A., Mangenot S., Cruveiller S., Barbe V., Duran R.,
RA Wu L.F., Talla E., Bonin P., Michotey V.;
RT "Genome sequence of the marine bacterium Marinobacter hydrocarbonoclasticus
RT SP17, which forms biofilms on hydrophobic organic compounds.";
RL J. Bacteriol. 194:3539-3540(2012).
RN [2]
RP FUNCTION, INTERACTION WITH AUPB, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 49840 / DSM 8798 / CIP 103578 / SP17;
RX PubMed=29871914; DOI=10.1128/mbio.00520-18;
RA Mounier J., Hakil F., Branchu P., Naitali M., Goulas P., Sivadon P.,
RA Grimaud R.;
RT "AupA and AupB are outer and inner membrane proteins involved in alkane
RT uptake in Marinobacter hydrocarbonoclasticus SP17.";
RL MBio 9:E00520-E00520(2018).
CC -!- FUNCTION: Required for growth on alkanes. Probably involved in the
CC uptake of micelle-solubilized alkanes. {ECO:0000269|PubMed:29871914}.
CC -!- SUBUNIT: Interacts with the inner membrane protein AupB.
CC {ECO:0000269|PubMed:29871914}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:29871914}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- INDUCTION: Expression increases during biofilm formation on n-
CC hexadecane. Forms an operon with aupB. {ECO:0000269|PubMed:29871914}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a lower rate of biofilm formation on
CC solid paraffin and on the liquid alkane n-hexadecane, while growth on
CC nonalkane substrates was not affected. Planktonic growth on water-
CC soluble substrates is not affected. Mutants are impaired in the
CC assimilation of n-hexadecane solubilized in surfactant micelles.
CC {ECO:0000269|PubMed:29871914}.
CC -!- SIMILARITY: Belongs to the OmpP1/FadL family. {ECO:0000305}.
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DR EMBL; FO203363; CCG93977.1; -; Genomic_DNA.
DR AlphaFoldDB; H8WEC1; -.
DR SMR; H8WEC1; -.
DR EnsemblBacteria; CCG93977; CCG93977; MARHY0478.
DR KEGG; mhc:MARHY0478; -.
DR PATRIC; fig|2743.3.peg.469; -.
DR HOGENOM; CLU_615101_0_0_6; -.
DR Proteomes; UP000007884; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR005017; OMPP1/FadL/TodX.
DR PANTHER; PTHR35093; PTHR35093; 1.
DR Pfam; PF03349; Toluene_X; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Membrane; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..452
FT /note="Alkane uptake protein A"
FT /id="PRO_5003616267"
SQ SEQUENCE 452 AA; 48605 MW; F099D805582FED25 CRC64;
MSERSVYMVL SPRFSVRAVS LAVAAVSASL SMPTSASMGN LGTSYGVMPV DVATAQSLSM
FNEQVSATYY NPAALTKDPR GELTAGILHS EQELRSDNPN ASGDIVSDSP SQHVLIGMKT
NLGSLTRFGH PIYLGFIAGV EKYGKEMLAF SSETSESGQF LQYGKEPLFL NIGGATPIWR
GISAGASVRV TLEATANLDA VSTLGGETSR ERLAVNAEPS LKTILGTNID LGSTFCPESD
CFLNGWETAL TYRTKSSAST TVDSNIIVTQ TIPDPGLSLA VTTIDSFQPE TIAIGTQYSG
DGWRIGGSIE QQNWSELEDE FSGDSIKDQG SVASGNRIGF DDILIPRLGA EYQLNKNFAV
RGGVAYEESP LKTTRNPELN YLDTDKLVVG LGISATYDRT RLLAYPVRLD LGYQYQQLQE
RDFTVVDYDG DETSVTADGD IHVFSGSITL KF