SECA_MESH2
ID SECA_MESH2 Reviewed; 983 AA.
AC Q601A7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=mhp295;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV27504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE017332; AAV27504.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011206132.1; NC_006360.1.
DR AlphaFoldDB; Q601A7; -.
DR SMR; Q601A7; -.
DR STRING; 295358.mhp295; -.
DR EnsemblBacteria; AAV27504; AAV27504; mhp295.
DR KEGG; mhy:mhp295; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR Proteomes; UP000006822; 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; -; 3.
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 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; TIGR00963; 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; Translocase; Translocation; Transport.
FT CHAIN 1..983
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320854"
FT REGION 948..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 101..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 983 AA; 112323 MW; D330CED51EB444B1 CRC64;
MKNLFNFFKT SSELRLAYRL LKQINQKRSF YGAMTDFDLA NQTNIFKKRL ANGEKLKDIR
VDAFAVAREA TKRILGKTPY DVQILGGLIL DMGSVAEMKT GEGKTIASIP PVYLNALLGQ
GVIVSTVNEY LAERDAEDNG KVYNFLGLTV GINKTEMDAN TKRMMYNADI TYSVHSELGF
DYLRDNMVFS AAEKVQRGLN FCLIDEVDSI LIDEAKTPLI ISGGKTNLPA QYLSANQFVN
TLIAEDFYID EETKGIKLND KGIDKANAFF GLRNLYEIQN SEIVHRIQNA LRANKVMKRD
VEYIVQDGKI ALVDQFTGRI MAGRSYSEGL QQALQAKEGL EIEPETKTLA TITYQNFFRL
FKKLSGMTGT AKTEEQEFID VYNMRVNVIP TNKPMIRKDE RDEIFATSHE KNQAIISEVE
RVHKRGQPIL IGTSQVVDSE TLSEMLNQKG LYHTVLNAKQ NQLEAEIIAK AGRKNAITIA
TNMAGRGTDI ILEPGVTELG GLYILGTDKA EARRIDNQLR GRSGRQGDVG ISRFFISLQD
QLFRRFTNFD QIFGAYGQTN GAIKGKYIHA VLLAAQKKIE GFNFDMRKTV LSYDDVIRQQ
RDLIYAQRDI LLQIENFDHY IQKMIIRAVD IILNYDFIIL PNQEIHYKNL INFLNDNLSR
ITHFNFGQIG IENYPIEQLN EFLIKQLETI YFKQIQSVLK ENLGKTYFES ERYIILSTLD
SQWQNHIDTI DKLRSSANLV QYSQKNPYQI FTEEATKKFN ILVAESAYQA IVSLFNNSNA
EKIEYIKAIL SDGTAISYPA DSPQEIIDQI IASNEERIAA ARKAKEEKQP EFIEKQLAKL
KIEKVESGEE FELWKIGDSK LVNLKKEMPL DEKQNILVKM QQEQLEMMSE EEKNLIQEQN
LEIVEIEEIE EEIQNENPQK VEFVDFKNDP DAYNKLIFGA DYADKQLISS EEEDNNEKTN
INNNEDLERT KGEAQQTAKN PNE
