ID   SECA_MALP2              Reviewed;        1405 AA.
AC   Q8EVL6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
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=MYPE5470;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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, ECO:0000305}.
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DR   EMBL; BA000026; BAC44337.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EVL6; -.
DR   SMR; Q8EVL6; -.
DR   STRING; 272633.26454007; -.
DR   PRIDE; Q8EVL6; -.
DR   EnsemblBacteria; BAC44337; BAC44337; BAC44337.
DR   KEGG; mpe:MYPE5470; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_254030_0_0_14; -.
DR   Proteomes; UP000002522; 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..1405
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000321058"
FT   REGION          1..1099
FT                   /note="Protein translocase subunit SecA"
FT   REGION          1100..1405
FT                   /note="Unknown"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         106..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1405 AA;  162039 MW;  D659050B0172A958 CRC64;
     MHMKIKKFKK IKKKSKILVK AKLIAQQVEN NREEYSALSI EDLRIRTDYL VDGLAKDKFT
     LEDIIVDALS IAREIIYREH GMLAYEVQMM GAYVVHTGDF AEMYTGEGKS LTLLLVSFVN
     ALTKRGVHIV TVNEYLVERD ALFAQKAFEK LGITVGYNTS KLSKATKKEM FARDITYTTN
     SELGFDYLKD NMVRDINEKV IRELFFVIVD EADSVLIDEA RTPLIISGQP KEDFSLYLDI
     DKFVGSLAED DYKIDNESNT IALTDQGVSK AEKFFNLTNL YSVESAEIVH KITNSLVAHY
     IFANGKEYLV KDDKIYLVDQ FTGRVLEGRS YNAGLQQAIQ AKERVTIEPE NVVMATITYQ
     SFFRLYEKLS GVSGTAMTEA EEFLKIYNMV VVRIPTNKPV ARIDKQDYIF GTKRVKWNHV
     IQEIVNRHET GQPILVGTAS VTDSEIIHER LTELKIPHEV LNARDNTKEA EIVKHAGEKG
     AITISTNMAG RGTDIKVSDE IRELGGLYVI GTERHESRRI DNQLRGRTGR QGDPGESRFF
     TSLEDALFKR FATDRFEKAS QKLEEEFYDS RFFSKMLDRT QKKVEGLNFD IRKNLMDYDH
     VLSLQRELIY KQRDQILLKT NNLNIINNMI DDYVETEILN FKNNDNTSLV DANKIVAFLN
     EKILKFSYFT PATFANMPIL LAIDKAISII KKVVDVKCKI LEKINGLNVI DEILLVNLDQ
     KWTTHIDKMT KLREGVNLRS LEQRSPLNIY IEDGNNLFER MKINVVTDTI TSICNLSLPN
     EMIEITNALD EFVNSEEFKK KNYGNQREIE QNFNSALSFS GSATSEFDNF IESELENTLI
     EETPEEYVEV EEYIPQQTEP EVVETETTPY GFEIPKYDTS GTDKYELNNG SSEVNILENE
     SDIFENSFSQ IQNTFNTEEL DPQETPHTAK ADDQFVFESA NLEDDIEEIE NVSNIDKAPE
     IQQPLSEEEI QKILDMPAFK DDEKPLTIGN YLDNILDSMD IDYDQDKEIT QQLEPSSNEQ
     EVTANIPEQN QLDITTSDID NEIELLDESE RESIKEEIQK SISFDLSNDP DFIEYRNSVF
     VNKNNGIDYS DYKKLNEDES DDDIKAFYKL PKVDKKEPGT LFGGNLLKKT PFNFKNKNEL
     DNEKIKSTNL FREENQASEQ ELNTLLQLDD EKDRLEKINQ LLNKEDPEVL ERKELERQVE
     FETPVYYLED IPEGESLDNF KAMDNPHEEQ SFEDNLVDEE NQQLEFEEAL DEVIDDGQFN
     DEVEAAELSE EVLEEVINPN PEELSEEDKW LITKKEHEKF MEKYLGDVKE LTSENPEVVT
     ALLQEKNKNL KDVEIIENNE ELENTNEEEP NINSQDSFLN NIKIIKTVDK ESEDETEIIQ
     EINQPAEIHN LQKDILDYLK ENNKK