ID A0A2N3PXF1_9PROT Unreviewed; 515 AA.
AC A0A2N3PXF1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Porin {ECO:0000256|RuleBase:RU364005};
GN ORFNames=CWS72_07760 {ECO:0000313|EMBL:PKU25092.1};
OS Telmatospirillum siberiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Telmatospirillum.
OX NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU25092.1, ECO:0000313|Proteomes:UP000233293};
RN [1] {ECO:0000313|Proteomes:UP000233293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA Pester M., Loy A.;
RT "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT cycling.";
RL Submitted (DEC-2017) 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:PKU25092.1}.
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DR EMBL; PIUM01000006; PKU25092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PXF1; -.
DR Proteomes; UP000233293; 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.
DR SUPFAM; SSF56935; Porins; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|RuleBase:RU364005};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000233293};
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..27
FT /evidence="ECO:0000256|RuleBase:RU364005"
FT CHAIN 28..515
FT /note="Porin"
FT /evidence="ECO:0000256|RuleBase:RU364005"
FT /id="PRO_5014487204"
FT COILED 29..63
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 515 AA; 54831 MW; 49887B641C31916A CRC64;
MPHMHKLKTL LIGSTAITCI LSLPAMASEA DLLKKIDALE AHIQEMQNTQ RQLRKELVEQ
SEANAAARAA VGRIEAIEKK AANDQATASA EVKAAVAKAE AVQKTSFAGD IPGSFKIPGT
ETSIKLGGAV KIDIADDLSN SLGGSATDWN GIGFKGSSTS HRGGQVQFTA RQSRLSLETY
TPSEVLGPVK AFFESDFYGG GGSYQGTVVG PNRRDTNSAY FRIRQAYVEA SDVLVGQTWS
TFMDMASSPE TLDIGGPPGF NNGIRQPMVR YSKKAGPGKL YLAVESPDGD FQGANQAQFA
TGASVPSTNS IDVAPDVVVK YEYKADWGQL TTSAVGRWQT ASAGGGTVVG SFNGRADAFG
YGALFGGLVR PVEGAKSGVQ FQVLGGNGIG RYMAPTTSTN YEYGAVVDQK NKSLESLFAW
GAGGGPKIYW ADQWRSSFIY GHSHVSNYHG LLPTSSLKNL DGFVANLLWS PFRNPASYIG
LEYTYAHVEN YTIPTAALSN KGDANRLQVS VQYAF
//
