LOLB_MARMS
ID LOLB_MARMS Reviewed; 192 AA.
AC A6W1C5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Outer-membrane lipoprotein LolB {ECO:0000255|HAMAP-Rule:MF_00233};
DE Flags: Precursor;
GN Name=lolB {ECO:0000255|HAMAP-Rule:MF_00233}; OrderedLocusNames=Mmwyl1_3602;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a critical role in the incorporation of lipoproteins in
CC the outer membrane after they are released by the LolA protein.
CC {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00233}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00233}.
CC -!- SIMILARITY: Belongs to the LolB family. {ECO:0000255|HAMAP-
CC Rule:MF_00233}.
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; CP000749; ABR72504.1; -; Genomic_DNA.
DR RefSeq; WP_012071269.1; NC_009654.1.
DR AlphaFoldDB; A6W1C5; -.
DR SMR; A6W1C5; -.
DR STRING; 400668.Mmwyl1_3602; -.
DR EnsemblBacteria; ABR72504; ABR72504; Mmwyl1_3602.
DR KEGG; mmw:Mmwyl1_3602; -.
DR eggNOG; COG3017; Bacteria.
DR HOGENOM; CLU_092816_2_1_6; -.
DR OMA; YQTRGSF; -.
DR OrthoDB; 1797257at2; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd16326; LolB; 1.
DR HAMAP; MF_00233; LolB; 1.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR004565; OM_lipoprot_LolB.
DR Pfam; PF03550; LolB; 1.
DR SUPFAM; SSF89392; SSF89392; 1.
DR TIGRFAMs; TIGR00548; lolB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Protein transport; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT CHAIN 18..192
FT /note="Outer-membrane lipoprotein LolB"
FT /id="PRO_0000336611"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ SEQUENCE 192 AA; 21175 MW; 3BA71F1C9BE8F384 CRC64;
MTYRTLCILA FTALISACSS RPTGPTTPPP ESVSAISKWE TSGRVGIRTK NDAVSGNFNW
QKDPKTFALS IVGPFGQGAT HLNQSNDGVV TLAYEDTVVT GNNPETLLQQ ELGWEFPVNQ
VTYWIRGLAY PNSAAKISKD PDSQLPNKIE QDGWLITYSN FTKVDGLSLP QKMQVSNPPF
RVNLIINQWT IQ