SECY2_STRPN
ID SECY2_STRPN Reviewed; 405 AA.
AC Q97P79;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Accessory Sec system protein translocase subunit SecY2 {ECO:0000255|HAMAP-Rule:MF_01466};
GN Name=secY2 {ECO:0000255|HAMAP-Rule:MF_01466}; OrderedLocusNames=SP_1763;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP DISCUSSION OF SEQUENCE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=16861665; DOI=10.1128/iai.00316-06;
RA Obert C., Sublett J., Kaushal D., Hinojosa E., Barton T., Tuomanen E.I.,
RA Orihuela C.J.;
RT "Identification of a candidate Streptococcus pneumoniae core genome and
RT regions of diversity correlated with invasive pneumococcal disease.";
RL Infect. Immun. 74:4766-4777(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=18507531; DOI=10.1086/589775;
RA Rose L., Shivshankar P., Hinojosa E., Rodriguez A., Sanchez C.J.,
RA Orihuela C.J.;
RT "Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block
RT adhesion and protect mice against pneumococcal challenge.";
RL J. Infect. Dis. 198:375-383(2008).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=20714350; DOI=10.1371/journal.ppat.1001044;
RA Sanchez C.J., Shivshankar P., Stol K., Trakhtenbroit S., Sullam P.M.,
RA Sauer K., Hermans P.W., Orihuela C.J.;
RT "The pneumococcal serine-rich repeat protein is an intra-species bacterial
RT adhesin that promotes bacterial aggregation in vivo and in biofilms.";
RL PLoS Pathog. 6:E1001044-E1001044(2010).
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required for export of possible cell wall proteins. The central subunit
CC of a protein translocation channel. {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SUBUNIT: Component of the accessory SecA2/SecY2 protein translocase
CC complex required to export cell wall proteins. May form heterotrimers
CC with SecE and SecG subunits. {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01466};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- DISRUPTION PHENOTYPE: Deletion of 15 genes (from psrP, SP_1772 to
CC SP_1756, includes the accessory Sec export proteins SecA2 and SecY2)
CC and infection of female BALB/cJ mice, shows the psrP-secY2A2 region is
CC required for lung infection and for infection to progress to blood.
CC Mice infected intraperitoneally showed wild-type infection. Decreased
CC adherence to lung but not pharynx or brain cells. The psrP-secY2A2
CC region deletion has no effect on bacterial growth rate, capsule levels,
CC autolysis, or transformation (PubMed:18507531). In vitro significantly
CC decreased biofilm formation is seen; the large deletion mutant (SP_1772
CC to SP_1756) is no more affected than the single psrP deletion
CC (PubMed:20714350). {ECO:0000269|PubMed:18507531,
CC ECO:0000269|PubMed:20714350}.
CC -!- MISCELLANEOUS: Encoded in RD10, a pathogenicity island with an atypical
CC GC content that is associated with invasive pneumococcal disease.
CC Pathogenicity islands account for greater than half the genomic
CC diversity observed between isolates (PubMed:11463916, PubMed:16861665).
CC The main function of this island seems to be correct synthesis and
CC export of pneumococcal serine-rich repeat protein PsrP
CC (PubMed:18507531, PubMed:20714350). {ECO:0000269|PubMed:18507531,
CC ECO:0000269|PubMed:20714350, ECO:0000303|PubMed:11463916,
CC ECO:0000303|PubMed:16861665}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01466}.
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DR EMBL; AE005672; AAK75838.1; -; Genomic_DNA.
DR PIR; E95205; E95205.
DR RefSeq; WP_000161876.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97P79; -.
DR SMR; Q97P79; -.
DR STRING; 170187.SP_1763; -.
DR EnsemblBacteria; AAK75838; AAK75838; SP_1763.
DR KEGG; spn:SP_1763; -.
DR eggNOG; COG0201; Bacteria.
DR OMA; YSYLEIM; -.
DR PhylomeDB; Q97P79; -.
DR BioCyc; SPNE170187:G1FZB-1788-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01466; SecY2; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR014269; SecY2.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR02920; acc_sec_Y2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..405
FT /note="Accessory Sec system protein translocase subunit
FT SecY2"
FT /id="PRO_0000414878"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
SQ SEQUENCE 405 AA; 45367 MW; C3A7D0501C1810BF CRC64;
MTKIYSSIAV KKGLFTSFLL FIYVLGSRII LPFVDLNTKD FLGGSTAYLA FSAALTGGNL
RSLSIFSVGL SPWMSAMILW QMFSFSKRLG LTSTSIEIQD RRKMYLTLLI AVIQSLAVSL
RLPVQSSYSA ILVVLMNTIL LIAGTFFLVW LSDLNASMGI GGSIVILLSS MVLNIPQDVL
ETFQTVHIPT GIIVLLALLT LVFSYLLALM YRARYLVPVN KIGLHNRFKR YSYLEIMLNP
AGGMPYMYVM SFLSVPAYLF ILLGFIFPNH SGLAALSKEF MVGKPLWVYV YISVLFLFSI
IFAFVTMNGE EIADRMKKSG EYIYGIYPGA DTSRFINRLV LRFSVIGGLF NVIMAGGPML
FVLFDEKLLR LAMIPGLFMM FGGMIFTIRD EVKALRLNET YRPLI
