OMP4_NEIMB
ID OMP4_NEIMB Reviewed; 242 AA.
AC P0A0V3; P38367;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Outer membrane protein class 4 {ECO:0000303|PubMed:2499543};
DE AltName: Full=Reduction-modifiable protein M {ECO:0000303|PubMed:2499543};
DE Short=RmpM {ECO:0000303|PubMed:2499543};
DE Flags: Precursor;
GN Name=rmpM {ECO:0000303|PubMed:2499543}; OrderedLocusNames=NMB0382;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=8765 / Serogroup B / Serotype 15,
RC CCUG 18241 / M986 / Serogroup B / Serotype 2, and
RC CCUG 37602 / M1080 / Serogroup B / Serotype 1;
RX PubMed=2499543; DOI=10.1128/iai.57.7.2066-2071.1989;
RA Klugman K.P., Gotschlich E.C., Blake M.S.;
RT "Sequence of the structural gene (rmpM) for the class 4 outer membrane
RT protein of Neisseria meningitidis, homology of the protein to gonococcal
RT protein III and Escherichia coli OmpA, and construction of meningococcal
RT strains that lack class 4 protein.";
RL Infect. Immun. 57:2066-2071(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP BIOTECHNOLOGY.
RX PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT "Characterization of the protein content of a meningococcal outer membrane
RT vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT spectrometry.";
RL Hum. Vaccin. 1:80-84(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR
RP LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
RN [5] {ECO:0007744|PDB:1R1M}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 87-242, SUBUNIT, DOMAIN,
RP DISULFIDE BOND, AND PROBABLE PETIDOGYLCAN-BINDING.
RC STRAIN=ATCC 53415 / Serogroup B;
RX PubMed=14763978; DOI=10.1111/j.1365-2958.2003.03903.x;
RA Grizot S., Buchanan S.K.;
RT "Structure of the OmpA-like domain of RmpM from Neisseria meningitidis.";
RL Mol. Microbiol. 51:1027-1037(2004).
CC -!- SUBUNIT: The C-terminus exists in a monomer-dimer equilibrium.
CC {ECO:0000269|PubMed:14763978}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P0A910}; Multi-pass membrane protein.
CC -!- DOMAIN: The periplasmic C-terminus (residues 87-242) probably binds
CC peptidoglycan. {ECO:0000305|PubMed:14763978}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when deleted in strains CCUG
CC 37602 / M1080 / Serogroup B / Serotype 1 and 8765 / Serotype 15.
CC {ECO:0000269|PubMed:2499543}.
CC -!- BIOTECHNOLOGY: Present in outer membrane vesicle blebs which are used
CC as vaccines in human. {ECO:0000269|PubMed:16645985,
CC ECO:0000269|PubMed:17038831}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF40822.1; -; Genomic_DNA.
DR PIR; A37004; A37004.
DR PIR; C81205; C81205.
DR RefSeq; NP_273431.1; NC_003112.2.
DR RefSeq; WP_002212455.1; NC_003112.2.
DR PDB; 1R1M; X-ray; 1.90 A; A=87-242.
DR PDBsum; 1R1M; -.
DR AlphaFoldDB; P0A0V3; -.
DR SMR; P0A0V3; -.
DR STRING; 122586.NMB0382; -.
DR PaxDb; P0A0V3; -.
DR EnsemblBacteria; AAF40822; AAF40822; NMB0382.
DR GeneID; 61282011; -.
DR KEGG; nme:NMB0382; -.
DR PATRIC; fig|122586.8.peg.483; -.
DR HOGENOM; CLU_016890_5_0_4; -.
DR OMA; CWRTGYW; -.
DR Proteomes; UP000000425; Chromosome.
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:ion transport; IEA:UniProtKB-KW.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Ion transport; Membrane;
KW Porin; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..242
FT /note="Outer membrane protein class 4"
FT /id="PRO_0000020112"
FT REPEAT 69..70
FT /note="1"
FT REPEAT 71..72
FT /note="2"
FT REPEAT 73..74
FT /note="3"
FT REPEAT 75..76
FT /note="4"
FT REPEAT 77..78
FT /note="5"
FT REPEAT 79..80
FT /note="6"
FT REPEAT 81..82
FT /note="7"
FT DOMAIN 92..229
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 69..82
FT /note="7 X 2 AA tandem repeats of X-P"
FT DISULFID 191..214
FT /evidence="ECO:0000269|PubMed:14763978"
FT VARIANT 78..79
FT /note="Missing (in strain: CCUG 18241)"
FT VARIANT 128..129
FT /note="SR -> GQ (in strain: CCUG 18241)"
FT VARIANT 132
FT /note="V -> I (in strain: CCUG 18241)"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1R1M"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:1R1M"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1R1M"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1R1M"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1R1M"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:1R1M"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1R1M"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:1R1M"
SQ SEQUENCE 242 AA; 26185 MW; 5E108F6D99C1B9E7 CRC64;
MTKQLKLSAL FVALLASGTA VAGEASVQGY TVSGQSNEIV RNNYGECWKN AYFDKASQGR
VECGDAVAAP EPEPEPEPAP APVVVVEQAP QYVDETISLS AKTLFGFDKD SLRAEAQDNL
KVLAQRLSRT NVQSVRVEGH TDFMGSDKYN QALSERRAYV VANNLVSNGV PVSRISAVGL
GESQAQMTQV CEAEVAKLGA KVSKAKKREA LIACIEPDRR VDVKIRSIVT RQVVPAHNHH
QH
