LPTD_ACIAD
ID LPTD_ACIAD Reviewed; 819 AA.
AC Q6F9W4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE Flags: Precursor;
GN Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA;
GN OrderedLocusNames=ACIAD2371;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Together with LptE, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01411}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptE and LptA. {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
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DR EMBL; CR543861; CAG69149.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F9W4; -.
DR SMR; Q6F9W4; -.
DR STRING; 62977.ACIAD2371; -.
DR EnsemblBacteria; CAG69149; CAG69149; ACIAD2371.
DR KEGG; aci:ACIAD2371; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_1_0_6; -.
DR OMA; DYSHLDW; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro.
DR GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR InterPro; IPR020889; LipoPS_assembly_LptD.
DR InterPro; IPR007543; LptD_C.
DR InterPro; IPR005653; OstA-like_N.
DR Pfam; PF04453; LptD; 1.
DR Pfam; PF03968; LptD_N; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Membrane; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT CHAIN 34..819
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000281584"
SQ SEQUENCE 819 AA; 93136 MW; F7697E2D25042EAC CRC64;
MRQMKYQFKF NPLAAAIFTL LCGGSMQSSY ADANDSASSV DNKKLKESIQ KAYPGQEFFE
QYYVEKSSPE AQVRDTRSLS SAFCTGTWIT PISPTTQAVP ADQATSVVTA DYAHYNPNGD
SELEGNVLID QQGRSIRANK VTIDRTQTYA NAEGNVQLAQ AGLLAQSDQI NYNLKTQQGD
LKNSFYISEQ QHAHGHAEQI QRTSPTEIIL RNATYTTCPP EQKPTWRLEA KEIKLNQDTG
RGTTKNTKLY VKDVPILAVP YFNFPIDNRR TTGILNPNIG FSNDGGLELT VPVYLNLAPN
YDATLTPRYI SDRGVMLQSE FRYLTENFGQ GKIWGGYLPD DKKYNNEDRK DFNLLHKWKI
NDYWSTDVEY HYASDKDYVT DLDTNPDSKT DLNLRRAWTL KYKNQIPGLT AQLKVEDFQT
LDKTVSDVDK PYARLPQFLL NYVTGNPLGL QYEFNNDTAY FKKNIDDAAN YSTQPSGTRI
YNQFATRYNF RTPWAFAIPE VSIRSINTFY DQNTVENLGL NSDNKSKSVV VPQFSLDTGL
IFQRDGDYLQ TITPRAFYAY APYKNQTGYP NFDTTSASIN YDQLFSPYRF YGHDRLEDNN
FLSLGVSYSL FDPQGLERLR AGVGQSFYFA DRRVTLNNTD DTIDTSKNSG PIVSISSQLT
NKFTVAANSA WMSNGDNAQH DFQTYYTGDH GNLYNLGYFN RKNIPDRQLA YDAAVASFVQ
PIMNNWRIMG HVQFDFRNNV AREYLLGVNY ESCCYAISVY GRSYYNDLDD PKDPNVNVKR
AVMAEITFKG LGGLNNKLAS LLENRVLGFK EINQSWTQR