SECA2_STAA8
ID SECA2_STAA8 Reviewed; 796 AA.
AC Q2FUW6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
GN OrderedLocusNames=SAOUHSC_02985;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ISP479C;
RX PubMed=18621893; DOI=10.1128/jb.00300-08;
RA Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL J. Bacteriol. 190:6188-6196(2008).
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required to export SraP, a serine-rich repeat cell wall protein encoded
CC upstream in the same operon. {ECO:0000269|PubMed:18621893}.
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 SraP. {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}.
CC -!- DISRUPTION PHENOTYPE: No effect on cell growth, significantly reduces
CC export of the cell wall protein SrpA. The small amount that is exported
CC seems to be glycosylated normally. {ECO:0000269|PubMed:18621893}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP000253; ABD31972.1; -; Genomic_DNA.
DR RefSeq; WP_000680947.1; NZ_LS483365.1.
DR RefSeq; YP_501434.1; NC_007795.1.
DR AlphaFoldDB; Q2FUW6; -.
DR SMR; Q2FUW6; -.
DR STRING; 1280.SAXN108_2920; -.
DR BindingDB; Q2FUW6; -.
DR ChEMBL; CHEMBL3832955; -.
DR EnsemblBacteria; ABD31972; ABD31972; SAOUHSC_02985.
DR GeneID; 3921467; -.
DR KEGG; sao:SAOUHSC_02985; -.
DR PATRIC; fig|93061.5.peg.2692; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; QRIDYPD; -.
DR PRO; PR:Q2FUW6; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..796
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318430"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 102..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 796 AA; 90930 MW; B36D057311959925 CRC64;
MKHKLDVTIN ELRLKSIRKI VKRINTWSDE VKSYSDDALK QKTIEFKERL ASGVDTLDTL
LPEAYAVARE ASWRVLGMYP KEVQLIGAIV LHEGNIAEMQ TGEGKTLTAT MPLYLNALSG
KGTYLITTND YLAKRDFEEM QPLYEWLGLT ASLGFVDIVD YEYQKGEKRN IYEHDIIYTT
NGRLGFDYLI DNLADSAEGK FLPQLNYGII DEVDSIILDA AQTPLVISGA PRLQSNLFHI
VKEFVDTLIE DVHFKMKKTK KEIWLLNQGI EAAQSYFNVE DLYSEQAMVL VRNINLALRA
QYLFESNVDY FVYNGDIVLI DRITGRMLPG TKLQAGLHQA IEAKEGMEVS TDKSVMATIT
FQNLFKLFES FSGMTATGKL GESEFFDLYS KIVVQVPTDK AIQRIDEPDK VFRSVDEKNI
AMIHDIVELH ETGRPVLLIT RTAEAAEYFS KVLFQMDIPN NLLIAQNVAK EAQMIAEAGQ
IGSMTVATSM AGRGTDIKLG EGVEALGGLA VIIHEHMENS RVDRQLRGRS GRQGDPGSSC
IYISLDDYLV KRWSDSNLAE NNQLYSLDAQ RLSQSNLFNR KVKQIVVKAQ RISEEQGVKA
REMANEFEKS ISIQRDLVYE ERNRVLEIDD AENQDFKALA KDVFEMFVNE EKVLTKSRVV
EYIYQNLSFQ FNKDVACVNF KDKQAVVTFL LEQFEKQLAL NRKNMQSAYY YNIFVQKVFL
KAIDSCWLEQ VDYLQQLKAS VNQRQNGQRN AIFEYHRVAL DSFEVMTRNI KKRMVKNICQ
SMITFDKEGM PVIHFP
