ID A0A1B9YJ31_9BRAD Unreviewed; 530 AA.
AC A0A1B9YJ31;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Porin {ECO:0000256|RuleBase:RU364005};
GN ORFNames=LMTR3_08060 {ECO:0000313|EMBL:OCK54756.1};
OS Bradyrhizobium sp. LMTR 3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK54756.1, ECO:0000313|Proteomes:UP000093220};
RN [1] {ECO:0000313|EMBL:OCK54756.1, ECO:0000313|Proteomes:UP000093220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK54756.1,
RC ECO:0000313|Proteomes:UP000093220};
RA Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA Martinez E.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms passive diffusion pores that allow small molecular
CC weight hydrophilic materials across the outer membrane.
CC {ECO:0000256|RuleBase:RU364005}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|RuleBase:RU364005}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU364005}.
CC -!- DOMAIN: Consists of 16-stranded beta-barrel sheets, with large surface-
CC exposed loops, that form a transmembrane pore at the center of each
CC barrel. The pore is partially ocluded by a peptide loop that folds into
CC the pore lumen. {ECO:0000256|RuleBase:RU364005}.
CC -!- SIMILARITY: Belongs to the alphaproteobacteria porin family.
CC {ECO:0000256|ARBA:ARBA00009521, ECO:0000256|RuleBase:RU364005}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCK54756.1}.
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; MAXC01000049; OCK54756.1; -; Genomic_DNA.
DR RefSeq; WP_065748279.1; NZ_MAXC01000049.1.
DR AlphaFoldDB; A0A1B9YJ31; -.
DR STRING; 189873.LMTR3_08060; -.
DR OrthoDB; 7801681at2; -.
DR Proteomes; UP000093220; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR003684; Porin_alphabac.
DR Pfam; PF02530; Porin_2; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|RuleBase:RU364005};
KW Ion transport {ECO:0000256|RuleBase:RU364005};
KW Membrane {ECO:0000256|RuleBase:RU364005};
KW Porin {ECO:0000256|RuleBase:RU364005};
KW Reference proteome {ECO:0000313|Proteomes:UP000093220};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364005};
KW Transmembrane {ECO:0000256|RuleBase:RU364005};
KW Transmembrane beta strand {ECO:0000256|RuleBase:RU364005};
KW Transport {ECO:0000256|RuleBase:RU364005}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU364005"
FT CHAIN 24..530
FT /note="Porin"
FT /evidence="ECO:0000256|RuleBase:RU364005"
FT /id="PRO_5009362316"
SQ SEQUENCE 530 AA; 55258 MW; EF5D6BA344ACA25F CRC64;
MKTARTLILS SAAGLIALSG AQAADLPVKA KAVEYVKICT LYGAGFFYIP GTDTCIKIGG
YLRADVTFNG GAHGAPAWSS DLGQQNRYRD YFVARSRMAL TIDTRTATEY GVVRTFGQGD
FQFNNFGSSN PSTLSAFPGG AANALSIPGG GYVAVEYLFI QFAGFTFGKS ASAYATPWQG
FPGNINSSLL GGQNTDTGVN NIQYTAEFGN GVSGSIGLDD PTVWDRTAVY NLSIPSAIGA
NGTGSNAYAG THAPDIVGRI RVDQAWGLFQ FSAAAHEVSG SYNTLGAGSV PNAFSEISGH
PESKWGGAVM AALQIKNIPT GAGDDIKLDV SYAKGATKYV IATSGSSPSF AMFGDSGFGY
QSVGFGATTD GVYFPGAAGT GGIALTTAWG VRGAFNHNWN PNWSTSLFGS YSAVRYDGGA
NDNLLGAGTS TAKGAYCAAF AASHPGQALA GNAAGNYTCN PDFNVSQLGV VTRWTPVKNL
TFSGEVQWFH LDQKMSGSSV FTAAAPKPNA LYEFKDQDTV LLQFRAQRNF
//
