SLAM1_NEIMB
ID SLAM1_NEIMB Reviewed; 488 AA.
AC Q9K165;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Surface lipoprotein assembly modifier 1 {ECO:0000303|PubMed:27572441};
DE Short=Slam1 {ECO:0000303|PubMed:27572441};
DE AltName: Full=TPR repeat-containing protein NMB0313;
DE Flags: Precursor;
GN OrderedLocusNames=NMB0313;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3]
RP FUNCTION, INTERACTION WITH TBPB, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a, and MC58;
RX PubMed=27572441; DOI=10.1038/nmicrobiol.2016.9;
RA Hooda Y., Lai C.C., Judd A., Buckwalter C.M., Shin H.E., Gray-Owen S.D.,
RA Moraes T.F.;
RT "Slam is an outer membrane protein that is required for the surface display
RT of lipidated virulence factors in Neisseria.";
RL Nat. Microbiol. 1:16009-16009(2016).
CC -!- FUNCTION: Required for correct export to the cell surface of some cell
CC outer membrane lipoproteins both in Neisseria and heterologously in
CC E.coli. {ECO:0000269|PubMed:27572441}.
CC -!- SUBUNIT: Interacts with the C-terminal domain of surface lipoprotein
CC TbpB. {ECO:0000269|PubMed:27572441}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:27572441,
CC ECO:0000305|PubMed:17038831}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Consists of a soluble N-terminal domain and C-terminal probable
CC beta-barrel in the outer membrane with 14 predicted beta-strands
CC (Probable). Expression of just the C-terminal domain restores about 30%
CC levels of TbpB lipoprotein and nearly 100% levels of fHbp lipoprotein
CC on the cell surface in strains B16B6 and MC58, and confers surface
CC expression of lipoproteins TbpB, LbpB and fHbp, but not HpuA in E.coli
CC (PubMed:27572441). {ECO:0000269|PubMed:27572441,
CC ECO:0000305|PubMed:27572441}.
CC -!- DISRUPTION PHENOTYPE: Does not surface present lipoproteins TbpB, LbpB
CC or fHbp (in strains B16B6 and MC58). Bacteria are considerably less
CC virulent in mouse sepsis model (shown in strain B16B6 only).
CC {ECO:0000269|PubMed:27572441}.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human. {ECO:0000269|PubMed:17038831}.
CC -!- SIMILARITY: Belongs to the Slam family. {ECO:0000305}.
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DR EMBL; AE002098; AAF40758.1; -; Genomic_DNA.
DR PIR; G81213; G81213.
DR RefSeq; NP_273362.1; NC_003112.2.
DR RefSeq; WP_010980777.1; NC_003112.2.
DR AlphaFoldDB; Q9K165; -.
DR SMR; Q9K165; -.
DR STRING; 122586.NMB0313; -.
DR PaxDb; Q9K165; -.
DR EnsemblBacteria; AAF40758; AAF40758; NMB0313.
DR GeneID; 61282082; -.
DR KEGG; nme:NMB0313; -.
DR PATRIC; fig|122586.8.peg.396; -.
DR HOGENOM; CLU_034927_1_0_4; -.
DR OMA; FMPARNR; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR007655; Slam.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF04575; SlipAM; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Membrane; Reference proteome; Repeat; Signal;
KW TPR repeat; Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..488
FT /note="Surface lipoprotein assembly modifier 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000320328"
FT TRANSMEM 204..214
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..252
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..267
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..291
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..304
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..325
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..340
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..364
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..377
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..402
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..417
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..448
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..464
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..488
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT REPEAT 118..151
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 171..204
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REGION 32..202
FT /note="N-terminal domain"
FT /evidence="ECO:0000303|PubMed:27572441"
FT REGION 203..488
FT /note="C-terminal probable beta barrel, partially restores
FT export of lipoproteins"
FT /evidence="ECO:0000303|PubMed:27572441"
SQ SEQUENCE 488 AA; 56224 MW; 808FCE9C39A68AE9 CRC64;
MVIFYFCGKT FMPARNRWML LLPLLASAAY AEETPREPDL RSRPEFRLHE AEVKPIDREK
VPGQVREKGK VLQIDGETLL KNPELLSRAM YSAVVSNNIA GIRVILPIYL QQAQQDKMLA
LYAQGILAQA DGRVKEAISH YRELIAAQPD APAVRMRLAA ALFENRQNEA AADQFDRLKA
ENLPPQLMEQ VELYRKALRE RDAWKVNGGF SVTREHNINQ APKRQQYGKW TFPKQVDGTA
VNYRLGAEKK WSLKNGWYTT AGGDVSGRVY PGNKKFNDMT AGVSGGIGFA DRRKDAGLAV
FHERRTYGND AYSYTNGARL YFNRWQTPKW QTLSSAEWGR LKNTRRARSD NTHLQISNSL
VFYRNARQYW MGGLDFYRER NPADRGDNFN RYGLRFAWGQ EWGGSGLSSL LRLGAAKRHY
EKPGFFSGFK GERRRDKELN TSLSLWHRAL HFKGITPRLT LSHRETRSND VFNEYEKNRA
FVEFNKTF
