ID   LPTD_ACIB2              Reviewed;         818 AA.
AC   D0C7T1;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 51.
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, ECO:0000303|PubMed:26668262};
GN   ORFNames=HMPREF0010_00811 {ECO:0000312|EMBL:EEX05046.1};
OS   Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG
OS   19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=575584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC   109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC   109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=26668262; DOI=10.1128/jb.00639-15;
RA   Bojkovic J., Richie D.L., Six D.A., Rath C.M., Sawyer W.S., Hu Q.,
RA   Dean C.R.;
RT   "Characterization of an Acinetobacter baumannii lptD deletion strain:
RT   permeability defects and response to inhibition of lipopolysaccharide and
RT   fatty acid biosynthesis.";
RL   J. Bacteriol. 198:731-741(2015).
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   -!- DISRUPTION PHENOTYPE: Non-essential under typical in vitro growth
CC       conditions. Loss of lptD causes impaired in vitro growth. Decreases LPS
CC       levels and susceptibility to polymyxin B, increases outer membrane
CC       permeability and hypersensitivity to hydrophobic antibiotics. Causes an
CC       accumulation of lipid IV(A). Deletion impairs cell envelope integrity
CC       more than the loss of LPS biosynthesis, presumably due to the
CC       accumulation of toxic intermediates. {ECO:0000269|PubMed:26668262}.
CC   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
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; GG704572; EEX05046.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0C7T1; -.
DR   SMR; D0C7T1; -.
DR   EnsemblBacteria; EEX05046; EEX05046; HMPREF0010_00811.
DR   Proteomes; UP000005740; Unassembled WGS sequence.
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; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           34..818
FT                   /note="LPS-assembly protein LptD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT                   /id="PRO_0000439170"
SQ   SEQUENCE   818 AA;  92488 MW;  6FEF27F8BE21FFE7 CRC64;
     MVNETMKHQF KFNPLATAIF TLLCSGSIQS SYAESAGVVS NIDNNQLKAS IKEAYPGQEF
     FQQYYVDKSA PEAQLRNNKY LSSAFCQGTW ITPINPETKA LDADKATSVV TADYGHYNPA
     GDSVLEGNVV IDQEGRTVRA DKVTIDKTQT FAHAQGRVQL AQGGLLSQSD EIDYNLKTQT
     GNLDNSFYIS EQQHAHGHAG KIERTSPNVM VLNDATYTTC PPGQKPGWKI QANKIELNQE
     TGRGVTRGTK LYVKDVPVLA VPYFNFPIDD RRTTGILNPQ FGFSNDGGIE LSVPVYLNLA
     PNYDATITPR YLADRGAMLQ GEFRYLTDGF GAGQIWGGIL PSDKEYDDKD RKDFHFLHNW
     DINDQWSTNL EYNYASDKDY FSDLDSSPIS KTDLNLRRAW ELNYQHGIPG LKAQLKVEDF
     QTLDPEVKDV NKPYARLPQF LLNYVTGNPL GLQYEFNNDT AYFKKSINDD SAQESSGTRI
     YNQFATRYNY RTPAAFVIPE LSVRSIQTFY DKDSIASQGL DGGSENKSVV VPQFTLDTGL
     NFEREGKYLQ TLTPRAFYAY APYKNQDGYP NFDSTTASIS YDQLFNPYRF YGHDRLEDNN
     FLSLGVSYSL FDTVGLERLR ASVGQSYYFE DRRVTLKQQD EIDTERNTGP VVSLSSQLNQ
     NFTIAANSAW MSNGDNAQRD FQLYYTGDKG NLYNLGYFYR KDIPGRQDTY DQVVASFIQP
     IKDNWRIMGH VQYDMDNDVA RELLLGVNYE SCCWGISVYG RSYYNDLDDP KSPDVSEKRA
     IMAEITLKGL GGLNNKLASL LENRVLGFNK INQSWTQR