MSPA_MYCS2
ID MSPA_MYCS2 Reviewed; 211 AA.
AC A0QR29; I7G4H6; Q9RLP7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Porin MspA;
DE Flags: Precursor;
GN Name=mspA; OrderedLocusNames=MSMEG_0965, MSMEI_0939;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 28-72 AND 193-211,
RP FUNCTION AS A PORIN, MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=10476028; DOI=10.1046/j.1365-2958.1999.01472.x;
RA Niederweis M., Ehrt S., Heinz C., Kloecker U., Swiderek K., Riley L.W.,
RA Benz R.;
RT "Cloning of the mspA gene encoding a porin from Mycobacterium smegmatis.";
RL Mol. Microbiol. 33:933-945(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION IN CELL WALL, AND DISRUPTION PHENOTYPE.
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 [6]
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).
RN [7]
RP TOPOLOGY, DOMAIN, AND CYSTEINE SCANNING STUDIES.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16352610; DOI=10.1074/jbc.m511642200;
RA Mahfoud M., Sukumaran S., Hulsmann P., Grieger K., Niederweis M.;
RT "Topology of the porin MspA in the outer membrane of Mycobacterium
RT smegmatis.";
RL J. Biol. Chem. 281:5908-5915(2006).
RN [8]
RP FUNCTION IN PHOSPHATE UPTAKE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17209034; DOI=10.1128/jb.01600-06;
RA Wolschendorf F., Mahfoud M., Niederweis M.;
RT "Porins are required for uptake of phosphates by Mycobacterium smegmatis.";
RL J. Bacteriol. 189:2435-2442(2007).
RN [9]
RP FUNCTION IN ANTIBIOTIC UPTAKE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18559650; DOI=10.1128/aac.00239-08;
RA Danilchanka O., Pavlenok M., Niederweis M.;
RT "Role of porins for uptake of antibiotics by Mycobacterium smegmatis.";
RL Antimicrob. Agents Chemother. 52:3127-3134(2008).
RN [10]
RP FUNCTION IN IRON UPTAKE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20952578; DOI=10.1128/jb.00986-10;
RA Jones C.M., Niederweis M.;
RT "Role of porins in iron uptake by Mycobacterium smegmatis.";
RL J. Bacteriol. 192:6411-6417(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 28-211, SUBUNIT, SUBCELLULAR
RP LOCATION IN OUTER MEMBRANE, AND MUTAGENESIS OF GLY-96.
RX PubMed=14976314; DOI=10.1126/science.1094114;
RA Faller M., Niederweis M., Schulz G.E.;
RT "The structure of a mycobacterial outer-membrane channel.";
RL Science 303:1189-1192(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 28-207.
RX PubMed=18187656; DOI=10.1126/science.1150421;
RA Grueninger D., Treiber N., Ziegler M.O., Koetter J.W., Schulze M.S.,
RA Schulz G.E.;
RT "Designed protein-protein association.";
RL Science 319:206-209(2008).
CC -!- FUNCTION: The major porin in this organism, forms a water-filled
CC channel which favors the permeation of cations, amino acids, iron
CC Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the
CC predominant siderophore. Plays a role in transport of beta-lactamase
CC and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well
CC as chloramphenicol. There are about 2400 porins in wild-type, 800 in an
CC mspA deletion and 150 in a double mspA-mspC deletion. Different
CC conductance values with maxima at 2.3 and 4.6 nanosiemens might be
CC caused by a simultaneous reconstitution of MspA channels into the
CC membrane or by the existence of different MspA conformations.
CC {ECO:0000269|PubMed:10476028, ECO:0000269|PubMed:16238622,
CC ECO:0000269|PubMed:17209034, ECO:0000269|PubMed:18559650,
CC ECO:0000269|PubMed:20952578}.
CC -!- SUBUNIT: Forms very stable octamers. Isolated as a 100 kDa complex that
CC can be reduced to monomers upon boiling in 80% dimethyl sulfoxide for
CC 15 minutes. Structures show a goblet with the wide end on the exterior
CC of the outer membrane and a central channel. It is not known if mixed
CC oligomers of MspA with other Msp subunits form in vivo.
CC {ECO:0000269|PubMed:10476028, ECO:0000269|PubMed:14976314}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane. Secreted, cell wall.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:16238622}.
CC -!- DOMAIN: The rim domain (28-96 and 152-211) is accessible from the
CC external milieu and is partially embedded in the outer membrane. The
CC stem domain (131-148) is inaccessible from the outside and embedded in
CC the outer membrane, while loop 6 (121-127) is thought to be in the
CC periplasm. {ECO:0000269|PubMed:16352610}.
CC -!- MASS SPECTROMETRY: Mass=19406; Mass_error=2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10476028};
CC -!- DISRUPTION PHENOTYPE: Single deletion has decreased permeability to the
CC antibiotic cephaloridine (9-fold), glucose (4-fold), serine, phosphate
CC and iron Fe(3+). Growth rates are wild-type, due to the other Msp-type
CC porins. A double mspA-mspC deletion takes up less cephaloridine,
CC glucose, serine and phosphate than the single mspA deletion and grows
CC slower than wt or single mspA deletion. A triple mspA-mspC-mspD
CC deletion grows even slower and has reduced Fe(3+) transport compared to
CC wild-type. {ECO:0000269|PubMed:11309127, ECO:0000269|PubMed:16238622,
CC ECO:0000269|PubMed:17209034, ECO:0000269|PubMed:18559650,
CC ECO:0000269|PubMed:20952578}.
CC -!- SIMILARITY: Belongs to the mycobacterial porin (TC 1.B.24) family.
CC {ECO:0000305}.
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DR EMBL; AJ001442; CAB56052.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK74363.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37419.1; -; Genomic_DNA.
DR RefSeq; WP_011727317.1; NZ_SIJM01000010.1.
DR RefSeq; YP_885367.1; NC_008596.1.
DR PDB; 1UUN; X-ray; 2.50 A; A/B=28-211.
DR PDB; 2V9U; X-ray; 2.59 A; A/B/C/D/E/F/G/H=28-211.
DR PDBsum; 1UUN; -.
DR PDBsum; 2V9U; -.
DR AlphaFoldDB; A0QR29; -.
DR SMR; A0QR29; -.
DR STRING; 246196.MSMEI_0939; -.
DR TCDB; 1.B.24.1.1; the mycobacterial porin (mbp) family.
DR PRIDE; A0QR29; -.
DR EnsemblBacteria; ABK74363; ABK74363; MSMEG_0965.
DR EnsemblBacteria; AFP37419; AFP37419; MSMEI_0939.
DR GeneID; 66739130; -.
DR KEGG; msg:MSMEI_0939; -.
DR KEGG; msm:MSMEG_0965; -.
DR PATRIC; fig|246196.19.peg.953; -.
DR eggNOG; ENOG5031B57; Bacteria.
DR OMA; CMSKTAV; -.
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 GO; GO:0055072; P:iron ion homeostasis; 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 3D-structure; Cell outer membrane; Cell wall; Direct protein sequencing;
KW Ion transport; Iron; Iron transport; Membrane; Porin; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:10476028"
FT CHAIN 28..211
FT /note="Porin MspA"
FT /id="PRO_5000064285"
FT MUTAGEN 96
FT /note="G->R: Increases yield of ordered crystals."
FT /evidence="ECO:0000269|PubMed:14976314"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 42..55
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 65..79
FT /evidence="ECO:0007829|PDB:1UUN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1UUN"
FT TURN 124..129
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 153..178
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:1UUN"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1UUN"
SQ SEQUENCE 211 AA; 22118 MW; B4DEC5639904487A CRC64;
MKAISRVLIA MVAAIAALFT STGTSHAGLD NELSLVDGQD RTLTVQQWDT FLNGVFPLDR
NRLTREWFHS GRAKYIVAGP GADEFEGTLE LGYQIGFPWS LGVGINFSYT TPNILIDDGD
ITAPPFGLNS VITPNLFPGV SISADLGNGP GIQEVATFSV DVSGAEGGVA VSNAHGTVTG
AAGGVLLRPF ARLIASTGDS VTTYGEPWNM N
