ID A0A379C816_9PAST Unreviewed; 778 AA.
AC A0A379C816;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000256|HAMAP-Rule:MF_01411};
DE Flags: Precursor;
GN Name=lptD {ECO:0000256|HAMAP-Rule:MF_01411,
GN ECO:0000313|EMBL:SUB58522.1};
GN ORFNames=NCTC12872_00485 {ECO:0000313|EMBL:SUB58522.1};
OS Phocoenobacter uteri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Phocoenobacter.
OX NCBI_TaxID=146806 {ECO:0000313|EMBL:SUB58522.1, ECO:0000313|Proteomes:UP000255417};
RN [1] {ECO:0000313|EMBL:SUB58522.1, ECO:0000313|Proteomes:UP000255417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12872 {ECO:0000313|EMBL:SUB58522.1,
RC ECO:0000313|Proteomes:UP000255417};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with LptE, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane.
CC {ECO:0000256|HAMAP-Rule:MF_01411}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptE and LptA. {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01411}.
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DR EMBL; UGTA01000001; SUB58522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A379C816; -.
DR Proteomes; UP000255417; 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 Gene3D; 2.60.450.10; Lipopolysaccharide (LPS) transport protein A like domain; 1.
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 PANTHER; PTHR30189; LPS-ASSEMBLY PROTEIN; 1.
DR PANTHER; PTHR30189:SF1; LPS-ASSEMBLY PROTEIN LPTD; 1.
DR Pfam; PF04453; LptD; 1.
DR Pfam; PF03968; LptD_N; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_01411};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01411};
KW Reference proteome {ECO:0000313|Proteomes:UP000255417};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT CHAIN 26..778
FT /note="LPS-assembly protein LptD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT /id="PRO_5017090624"
FT DOMAIN 53..187
FT /note="Organic solvent tolerance-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03968"
FT DOMAIN 298..684
FT /note="LptD C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04453"
SQ SEQUENCE 778 AA; 90309 MW; C1D00ACB2547FC3A CRC64;
MMKDYRYTLL SLAIMTACAS QYANADLKTQ CRLGIPHFSG QIEQGEPETL PVYIEADKAT
ITELKEAVYS GSVLIKQGNR TINTQQFTVS QNPQNNRFAT LNNSFKYQDN YIRATGKKAS
IDLAGRKADL SNVDYQLVDK QGRGSAETIL LRDQVRRLKN ATYTACLPSD NAWQIDASEM
TQYIDKEYAE MWHARLKVGD VPIFYTPYLQ IPLGDRRRTG LLMPNYSHST KTGFTFHIPF
YLNIAPNMDA TITPTYYSRR GWQISPEFRY LTQLGQGTIA GEYMKKDRYE DWADKNQSRH
LFYWKHNASF LSDWRLSLDY TKVSDKQYLS HFDSSYGDST DGYVTQNVKF SYHQPNYNLS
IAGKKFQIFD TKNGAKPYRA LPQIEFNYYK NNIWKNADFS LFSQLTHFDN DSKEMPTAWR
LHIEPKLNLP LSNNYGSVNF ETKLYATQYW QKAGKEQKDK IKSHVTRVLP QFKVNFQTVL
ESDTQLISDF IQTLEPQIQY LYRPYKNQYD IGTTQYHSLG LGYDSMLRQQ DYFSLFSDRR
YSGLDRIASA NQITIGATTR FMKETTGQEY FNLSLGQIYY LSNSRIDDSS PNSNTDRSTS
WALETNWRFN KNWNLNGSYQ YDTRLDETSL ANLALQYKPQ NDKVVQFNYR YASQHYIDQN
LRSNQYGQDI KQLGVVLGWN INDNLSIMTS HYQDLALDKY VESQLGLTYN TCCWKATSYI
SRHLIPTPNG ERDDPTDVYY DNSIGVNFEL RFGSGYNTGV SKMLKKGLIP YTEEFDIN
//