ID SECA_MYCGE Reviewed; 806 AA.
AC P47318; Q49438;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=MG072;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-702 AND 757-806.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71290.1; -; Genomic_DNA.
DR EMBL; U01732; AAD10541.1; -; Genomic_DNA.
DR EMBL; U01743; AAD10553.1; -; Genomic_DNA.
DR PIR; I64207; I64207.
DR RefSeq; WP_009885928.1; NZ_AAGX01000011.1.
DR AlphaFoldDB; P47318; -.
DR SMR; P47318; -.
DR STRING; 243273.MG_072; -.
DR KEGG; mge:MG_072; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR InParanoid; P47318; -.
DR OrthoDB; 9805579at2; -.
DR BioCyc; MGEN243273:G1GJ2-84-MONOMER; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
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; 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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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; IPR020937; SecA_CS.
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 NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS01312; SECA; 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..806
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109593"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
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"
FT CONFLICT 494..497
FT /note="IRLG -> YPFS (in Ref. 2; AAD10541)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="S -> T (in Ref. 2; AAD10541)"
FT /evidence="ECO:0000305"
FT CONFLICT 610..618
FT /note="KQRDKFLLA -> TREVFIS (in Ref. 2; AAD10541)"
FT /evidence="ECO:0000305"
FT CONFLICT 624..625
FT /note="MI -> WS (in Ref. 2; AAD10541)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="L -> H (in Ref. 2; AAD10541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 91585 MW; FDD495AF98B1320F CRC64;
MAIFNFLKLI SPKNRILSKA NRIASEVESY KNYYRNLTDQ QLFEESNKLV DLVTKQNYTI
LDVCVAALAL IREVVYRETG EFAYRVQIIG AFIVLSGDFA EMMTGEGKTL TIVLAAYVSA
LEKRGVHVVT VNEYLAQRDA NNAMKILKRV GMSVGCNFAN LSPQLKQAAF NCDVTYTTNS
ELGFDYLRDN MVHSYQDKKI RELHFAIVDE GDSVLIDEAR TPLIISGPSK NEFGLYVAVD
RFVKSLTEQE FKIDPESRAA SLTELGIKKA EQTFKKENLF ALENSDLFHK IMNGLTAVKV
FEQGKEYIVR DGKVLIVDHF TGRILEGRSY SNGLQQAVQA KEYVEIEPEN VIVATITYQS
FFRLYNRLAA VSGTALTESE EFLKIYNMVV VPVPTNRPNI RKDRSDSVFG TPQIKWMAVV
KEIKKIHETS RPILIGTANI DDSELLHNLL LEANIPHEVL NAKNHSREAE IVTKAGQKNA
VTISTNMAGR GTDIRLGEGV AEMGGLYVLG TERNESRRID NQLRGRAARQ GDKGETKFFI
SLGDSLFKRF AHDKIERAIS KLGNETFDSA FFSKMLSRTQ KRVEAINFDT RKNLIDYDHV
LASQRELIYK QRDKFLLAND LSEMIDKMLE KFVQQFCDQY RNQKNQNLIN HIALAEALNL
EMNMQNTINP KVFENMTFDV AVDKTRNLVA KKISDKVNVL TKPIALNRFR DIIITSMDKH
WTEHLDSVFK LREGVVLRSM EHTSPLNVYI KETDILFKTM LQKIAQDVIV QIANLTTPDE
FDHSLMQANA LKKLAAIKAD EKSNQE
//
