SECA_MESFL
ID SECA_MESFL Reviewed; 943 AA.
AC Q6F260;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Mfl057;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017263; AAT75413.1; -; Genomic_DNA.
DR RefSeq; WP_011182954.1; NC_006055.1.
DR RefSeq; YP_053297.1; NC_006055.1.
DR AlphaFoldDB; Q6F260; -.
DR SMR; Q6F260; -.
DR STRING; 265311.Mfl057; -.
DR EnsemblBacteria; AAT75413; AAT75413; Mfl057.
DR GeneID; 2898182; -.
DR KEGG; mfl:Mfl057; -.
DR PATRIC; fig|265311.5.peg.57; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000006647; 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; 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; 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..943
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320848"
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 484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 943 AA; 106564 MW; A1D5C971AA40D65F CRC64;
MASDKSLLRM YGKYANEILS LEPEMKKLAN EDFAIKTQEL RDRIANGEHV DDLVVEAYAL
AREAANRVLG LNAYKVQLVG AIILHFGDIA EMRTGEGKTL TGLFPAYLNS LTGKGVHIVT
VNEYLSRRDS EINGQVFDLL GVSVGLNGTR MPKNLKREAY HADITYTTNA ELGFDYLRDN
MVVDKEHKVQ RELNFAIIDE ADSVLIDEAR TPLIISGGSS SRINLYKAAD EFAQKVNEKE
DIDIDLETKQ VYLTETGMKK AKDFFSLENL FALENTEIFH LILNALKAHF TFKEGVEYTV
ASGEVELIDQ FTGRILKGRA YSDGLQQAIQ AKEKVEIEEE TTTLATITYQ NFYRLYAKLS
GMTGTAKTEE EEFIKIYNTR VVVCPTNRPV IRKDEPDYTF GTKHAALKKL IQDIKTVNEI
GNPILIGTTS VESSEQIARY LEKAGLNFEM INAKNHDREA DIVSQAGQKY AITLATNMAG
RGTDIKLSQE VKDLGGLVVF GVERNEARRI DNQLRGRSGR QGDPGMSRFY ISMEDDLMIR
FASPRARKSF LSLGDEHIKS KFFTRAVTNA QKKLEGLNFD QRKNVLDYDN ILAQQREAMY
AQRDSILWAD NLKVVIKKFQ ITVAYEMIEE NSEIVHGEKT LNAEKLLKSI DGKLVAHKRF
VAKDFYNKEK MNLAVQLAEA MLEFYKARVI DIPDDVVLQM ERKNVLTSFD KYWTRHIDIA
SKLKAGIYLQ QYAQNNPLAV YVEQATELFN KTKIYIASEV VDVLSKIIIR DPEQNVESQK
IEITDEIIDD ILKSTGLTKA NINNKDINAK FDELIAKADN QNDIKKLSIQ RDIMLGLVIE
IQKRRENSGN KTVNLGKEEI DQMLAILGID NIGSTSKEEI ISKYEEKLKL AEDDKTKNLI
NIAKDVIIAL YEQIELIKKD ASSLKSVIDD DNDGGEVAKT RIG
