SECA2_STRPN
ID SECA2_STRPN Reviewed; 790 AA.
AC Q97P83;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=SP_1759;
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).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=28456649; DOI=10.1016/j.micinf.2017.04.003;
RA Bandara M., Skehel J.M., Kadioglu A., Collinson I., Nobbs A.H.,
RA Blocker A.J., Jenkinson H.F.;
RT "The accessory Sec system (SecY2A2) in Streptococcus pneumoniae is involved
RT in export of pneumolysin toxin, adhesion and biofilm formation.";
RL Microbes Infect. 19:402-412(2017).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. Has a central role in
CC coupling the hydrolysis of ATP to the transfer of proteins into and
CC across the cell membrane, serving as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across the
CC membrane. Plays a role in export of a number of proteins from the cell
CC including glycosylated PsrP and pneumolysin (ply) (PubMed:28456649).
CC {ECO:0000269|PubMed:28456649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- DISRUPTION PHENOTYPE: A single gene deletion has about 60% decreased
CC biofilm formation, 75% decreased adherence to human lung pneumocytes.
CC Has higher pneumolysin (ply) i.e. hemolytic activity in the cytoplasm
CC but less in the cell wall. Decreased levels of a number of cell wall
CC and secreted proteins (PubMed:28456649). Deletion of 15 genes (from
CC psrP, SP_1772 to SP_1756, includes the accessory Sec export proteins
CC SecA2 and SecY2) and infection of female BALB/cJ mice, shows the psrP-
CC secY2A2 region is required for lung infection and for infection to
CC progress to blood. Mice infected intraperitoneally showed wild-type
CC infection. Decreased adherence to lung but not pharynx or brain cells.
CC The psrP-secY2A2 region deletion has no effect on bacterial growth
CC rate, capsule levels, autolysis, or transformation (PubMed:18507531).
CC In vitro significantly decreased biofilm formation is seen; the large
CC deletion mutant (SP_1772 to SP_1756) is no more affected than the
CC single psrP deletion (PubMed:20714350). {ECO:0000269|PubMed:18507531,
CC ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:28456649}.
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 SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AE005672; AAK75834.1; -; Genomic_DNA.
DR PIR; A95205; A95205.
DR RefSeq; WP_000489782.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97P83; -.
DR SMR; Q97P83; -.
DR STRING; 170187.SP_1759; -.
DR EnsemblBacteria; AAK75834; AAK75834; SP_1759.
DR KEGG; spn:SP_1759; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; QRIDYPD; -.
DR PhylomeDB; Q97P83; -.
DR BioCyc; SPNE170187:G1FZB-1784-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR022490; SecA2.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR TIGRFAMs; TIGR03714; secA2; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..790
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318443"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 98..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 790 AA; 89741 MW; AA5F010D87A9A21A CRC64;
MFRRLGQDFQ LRKVKKILKQ INALKGKMSS LSDQELVAKT VEFRQRLSEG ESLDDILVEA
FAVVREADKR ILGMFPYDVQ VMGAIVMHYG NVAEMNTGEG KTLTATMPVY LNAFSGEGVM
VVTPNEYLSK RDAEEMGQVY RFLGLTIGVP FTEDPKKEMK AEEKKLIYAS DIIYTTNSNL
GFDYLNDNLA SNEEGKFLRP FNYVIIDEID DILLDSAQTP LIIAGSPRVQ SNYYAIIDTL
VTTLVEGEDY IFKEEKEEVW LTTKGAKSAE NFLGIDNLYK EEHASFARHL VYAIRAHKLF
TKDKDYIIRG NEMVLVDKGT GRLMEMTKLQ GGLHQAIEAK EHVKLSPETR AMASITYQSL
FKMFNKISGM TGTGKVAEKE FIETYNMSVV RIPTNRPRQR IDYPDNLYIT LPEKVYASLE
YIKQYHAKGN PLLVFVGSVE MSQLYSSLLF REGIAHNVLN ANNAAREAQI ISESGQMGAV
TVATSMAGRG TDIKLGKGVA ELGGLIVIGT ERMESQRIDL QIRGRSGRQG DPGMSKFFVS
LEDDVIKKFG PSWVHKKYKD YQVQDMTQPE VLKGRKYRKL VEKAQHASDS AGRSARRQTL
EYAESMNIQR DIVYKERNRL IDGSRDLEDV VVDIIERYTE EVAADHYASR ELLFHFIVTN
ISFHVKEVPD YIDVTDKTAV RSFMKQVIDK ELSEKKELLN QHDLYEQFLR LSLLKAIDDN
WVEQVDYLQQ LSMAIGGQSA SQKNPIVEYY QEAYAGFEAM KEQIHADMVR NLLMGLVEVT
PKGEIVTHFP
