ID D8MVV2_ERWBE Unreviewed; 116 AA.
AC D8MVV2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Outer membrane protein assembly factor BamE {ECO:0000256|HAMAP-Rule:MF_00925};
GN Name=smpA {ECO:0000313|EMBL:CAX60959.1};
GN Synonyms=bamE {ECO:0000256|HAMAP-Rule:MF_00925};
GN OrderedLocusNames=EbC_34280 {ECO:0000313|EMBL:CAX60959.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60959.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60959.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: Part of the outer membrane protein assembly complex, which is
CC involved in assembly and insertion of beta-barrel proteins into the
CC outer membrane. {ECO:0000256|HAMAP-Rule:MF_00925}.
CC -!- SUBUNIT: Part of the Bam complex, which is composed of the outer
CC membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE.
CC {ECO:0000256|HAMAP-Rule:MF_00925}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_00925}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00925}.
CC -!- SIMILARITY: Belongs to the BamE family. {ECO:0000256|HAMAP-
CC Rule:MF_00925}.
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DR EMBL; FP236843; CAX60959.1; -; Genomic_DNA.
DR RefSeq; WP_013203444.1; NC_014306.1.
DR AlphaFoldDB; D8MVV2; -.
DR STRING; 634500.EbC_34280; -.
DR KEGG; ebi:EbC_34280; -.
DR eggNOG; COG2913; Bacteria.
DR HOGENOM; CLU_083835_4_0_6; -.
DR Proteomes; UP000008793; 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:0051205; P:protein insertion into membrane; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1450.10; -; 1.
DR HAMAP; MF_00925; OM_assembly_BamE; 1.
DR InterPro; IPR026592; BamE.
DR InterPro; IPR037873; BamE-like.
DR InterPro; IPR007450; Lipoprotein_SmpA/OmlA.
DR PANTHER; PTHR37482; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAME; 1.
DR PANTHER; PTHR37482:SF1; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAME; 1.
DR Pfam; PF04355; SmpA_OmlA; 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_00925}; Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00925};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00925};
KW Palmitate {ECO:0000256|HAMAP-Rule:MF_00925};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00925}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..116
FT /note="Outer membrane protein assembly factor BamE"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009010192"
FT DOMAIN 35..104
FT /note="Lipoprotein SmpA/OmlA"
FT /evidence="ECO:0000259|Pfam:PF04355"
SQ SEQUENCE 116 AA; 12777 MW; 89B1B703A59E1A8F CRC64;
MRCKTLTAAA VVLLMMTAGC STLERVVYRP DINQGNYLVA NDVSKIHTGM TQQQVAYTLG
TPMMRDPFGS NVWYYVFRQE PGHEPVTQQT LTLTFDGSGT LTNIDNKPTL SGKKSG
//
