SECA2_STAA3
ID SECA2_STAA3 Reviewed; 796 AA.
AC Q2FDL0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SAUSA300_2584;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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. {ECO:0000255|HAMAP-Rule:MF_01382}.
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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP000255; ABD20912.1; -; Genomic_DNA.
DR RefSeq; WP_000680947.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FDL0; -.
DR SMR; Q2FDL0; -.
DR PRIDE; Q2FDL0; -.
DR EnsemblBacteria; ABD20912; ABD20912; SAUSA300_2584.
DR KEGG; saa:SAUSA300_2584; -.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; QRIDYPD; -.
DR Proteomes; UP000001939; 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..796
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318431"
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
