MSPB_MYCS2
ID MSPB_MYCS2 Reviewed; 215 AA.
AC A0QPU4; I7FDK5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Porin MspB;
DE Flags: Precursor;
GN Name=mspB; OrderedLocusNames=MSMEG_0520, MSMEI_0507;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PROTEIN SEQUENCE OF 32-51 AND 210-214, FUNCTION AS A PORIN, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION IN CELL WALL.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=11309127; DOI=10.1046/j.1365-2958.2001.02394.x;
RA Stahl C., Kubetzko S., Kaps I., Seeber S., Engelhardt H., Niederweis M.;
RT "MspA provides the main hydrophilic pathway through the cell wall of
RT Mycobacterium smegmatis.";
RL Mol. Microbiol. 40:451-464(2001).
RN [5]
RP FUNCTION AS A PORIN, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16238622; DOI=10.1111/j.1365-2958.2005.04878.x;
RA Stephan J., Bender J., Wolschendorf F., Hoffmann C., Roth E., Mailander C.,
RA Engelhardt H., Niederweis M.;
RT "The growth rate of Mycobacterium smegmatis depends on sufficient porin-
RT mediated influx of nutrients.";
RL Mol. Microbiol. 58:714-730(2005).
CC -!- FUNCTION: A backup porin induced when MspA, the major porin, is
CC deleted. Probably forms a water-filled channel which favors the
CC permeation of cations. There are about 2400 porins in wild-type, 800 in
CC an mspA deletion and 150 in a double mspA-mspC deletion. A triple mspA-
CC mspC-mspD deletion mutant has low but detectable channel activity.
CC Different conductance values with maxima at 2.3 and 4.6 nanosiemens
CC might be caused by a simultaneous reconstitution of MspB channels into
CC the membrane or by the existence of different MspB conformations.
CC {ECO:0000269|PubMed:11309127, ECO:0000269|PubMed:16238622}.
CC -!- SUBUNIT: Octamers. Probably forms a goblet with the wide end on the
CC exterior of the outer membrane and a central channel. It is not known
CC if mixed oligomers of MspB with other Msp subunits form in vivo (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. Secreted, cell
CC wall {ECO:0000269|PubMed:11309127}.
CC -!- INDUCTION: Not expressed in wild-type cells, it is induced in an mspA
CC deletion mutant. {ECO:0000269|PubMed:16238622}.
CC -!- MASS SPECTROMETRY: Mass=19406; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11309127};
CC -!- DISRUPTION PHENOTYPE: Single deletion is viable, and shows no effects
CC on glucose uptake. {ECO:0000269|PubMed:16238622}.
CC -!- SIMILARITY: Belongs to the mycobacterial porin (TC 1.B.24) family.
CC {ECO:0000305}.
CC -!- CAUTION: It is not clear if the data in PubMed:11309127 refer to MspB
CC or MspC as they are nearly identical. {ECO:0000305}.
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DR EMBL; CP000480; ABK73437.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36988.1; -; Genomic_DNA.
DR RefSeq; WP_003891919.1; NZ_SIJM01000025.1.
DR RefSeq; YP_884932.1; NC_008596.1.
DR AlphaFoldDB; A0QPU4; -.
DR SMR; A0QPU4; -.
DR STRING; 246196.MSMEI_0507; -.
DR EnsemblBacteria; ABK73437; ABK73437; MSMEG_0520.
DR EnsemblBacteria; AFP36988; AFP36988; MSMEI_0507.
DR GeneID; 66738700; -.
DR KEGG; msg:MSMEI_0507; -.
DR KEGG; msm:MSMEG_0520; -.
DR PATRIC; fig|246196.19.peg.516; -.
DR eggNOG; ENOG5031B57; Bacteria.
DR OMA; MKFIARG; -.
DR OrthoDB; 1579896at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR InterPro; IPR015286; Porin_fam_mycobact-type.
DR Pfam; PF09203; MspA; 1.
DR SUPFAM; SSF56959; SSF56959; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Cell wall; Direct protein sequencing; Ion transport;
KW Membrane; Porin; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000305|PubMed:11309127"
FT CHAIN 32..215
FT /note="Porin MspB"
FT /id="PRO_0000415940"
SQ SEQUENCE 215 AA; 22462 MW; 25E8F61B254F1307 CRC64;
MTAFKRVLIA MISALLAGTT GMFVSAGAAH AGLDNELSLV DGQDRTLTVQ QWDTFLNGVF
PLDRNRLTRE WFHSGRAKYI VAGPGADEFE GTLELGYQIG FPWSLGVGIN FSYTTPNILI
DDGDITAPPF GLNSVITPNL FPGVSISADL GNGPGIQEVA TFSVDVSGPA GGVAVSNAHG
TVTGAAGGVL LRPFARLIAS TGDSVTTYGE PWNMN
