SECA2_STRGN
ID SECA2_STRGN Reviewed; 793 AA.
AC Q9AET6;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 90.
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};
OS Streptococcus gordonii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA Bensing B.A., Sullam P.M.;
RT "An accessory sec locus of Streptococcus gordonii is required for export of
RT the surface protein GspB and for normal levels of binding to human
RT platelets.";
RL Mol. Microbiol. 44:1081-1094(2002).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=14729688; DOI=10.1128/jb.186.3.638-645.2004;
RA Bensing B.A., Gibson B.W., Sullam P.M.;
RT "The Streptococcus gordonii platelet binding protein GspB undergoes
RT glycosylation independently of export.";
RL J. Bacteriol. 186:638-645(2004).
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required to export GspB, a serine-rich repeat cell wall protein encoded
CC upstream in the same operon. {ECO:0000269|PubMed:12010500,
CC ECO:0000269|PubMed:14729688}.
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 (Potential). Part of the accessory
CC SecA2/SecY2 protein translocation apparatus required to export cell
CC wall protein GspB. {ECO:0000305}.
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, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Loss of export of cell wall protein GspB;
CC glycosylated GspB accumulates in the cytoplasm.
CC {ECO:0000269|PubMed:12010500, ECO:0000269|PubMed:14729688}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000305}.
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DR EMBL; AY028381; AAK17001.2; -; Genomic_DNA.
DR RefSeq; WP_061598997.1; NZ_LAWL01000014.1.
DR AlphaFoldDB; Q9AET6; -.
DR SMR; Q9AET6; -.
DR TCDB; 3.A.5.10.1; the general secretory pathway (sec) family.
DR PRIDE; Q9AET6; -.
DR BRENDA; 7.4.2.5; 5934.
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..793
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000414187"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 95..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 793 AA; 91152 MW; EA4B5BA0744A372C CRC64;
MVKNFFHIRR LKKILAKIKS FEKEMSSLSD LDLQKKTDEF KKRLADGENL DQLLPEAYAV
VREVDKRILG LFPYDVQVMG AIVLHEGNIA EMATGEGKTL TATMPLYLNA LSGQGAMLVT
PNSYLALRDA KEMGPVYRFL GLTIETAVRA DESKPLETKE KRRIYQADII YTTNSALGFD
YLIENLAENK KNQFLREFNY VIIDEIDSIL LDSAQTPLII SGAPRVQSNF YDMMNTLVQT
LYEDEDYCYD DEKNEVWLTQ KGIRAAESFL GLNHLFSKEN QELVRHLNLA LRAHMVYKKD
QDYVVRQSEN EAEVVLLDRA TGRLMELTRL QGGQHQAIEA KEHVKLTQET RAMASITYQN
LFKLFRKLSG MTGTGKVVES EFLETYSMSV VKIPTNCPVI RRDYPDQIYQ TLPEKVFASL
DEVKHYHAKG NPLLIFTGSV EMSEIYSSLL LREGIAHNLL NANNVAREAQ MIAESGQLGA
VTVATSMAGR GTDIKLGPGV ADLGGLVVIG TERMENHRID LQIRGRSGRQ GDPGISKFFI
SLEDDLLKKW GPDWIKNFYR DYSPEDFKNN PILLKQRRFK KLVSKAQKAS EGNAKLSRRL
TLEYAQSMKI QRELTYAERN RLLEDTNEME EEINRVIEYV IKQVAYEQSF ENRADFYRFI
LHHFSNRAER IPQEFDIHSP KEVSHLLQAI AEQELLAKKS YLKSDKLYSQ FQRLAILKAI
DENWVEQVDY LQQLKSALSG FHTSNKKPIV EYYQEAYDGF EYMKERMKHQ IVKNLLMSEL
ALNPKGEVVM YFP
