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Database: UniProt
Entry: E1QMH8_DESB2
LinkDB: E1QMH8_DESB2
Original site: E1QMH8_DESB2 
ID   E1QMH8_DESB2            Unreviewed;       839 AA.
AC   E1QMH8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
DE            EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN   OrderedLocusNames=Deba_2868 {ECO:0000313|EMBL:ADK86221.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK86221.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK86221.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01382};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:0000256|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}.
CC       Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC       50. {ECO:0000256|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC       ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
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DR   EMBL; CP002085; ADK86221.1; -; Genomic_DNA.
DR   RefSeq; WP_013259659.1; NC_014365.1.
DR   AlphaFoldDB; E1QMH8; -.
DR   STRING; 644282.Deba_2868; -.
DR   KEGG; dbr:Deba_2868; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_7; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000009047; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; IPR004027; SEC_C_motif.
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; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR   PANTHER; PTHR30612:SF0; SI:DKEY-187J14.7-RELATED; 1.
DR   Pfam; PF21090; P-loop_SecA; 2.
DR   Pfam; PF02810; SEC-C; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01382}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          3..572
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          89..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          416..588
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          785..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         105..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   839 AA;  94404 MW;  5FBC098E3F914A8C CRC64;
     MLGKIVKSIF GTKNDREIKR LGPLLEAINA FEPKMQALGD AELAALTPAF RQRLDNGQSL
     DDLLPEAFAA VREAGRRTLG QRHYDAQMIG GMVLHQGKIA EMKTGEGKTL AATLPVYLNA
     LAGRGVHVVT VNDYLARRDA EWMGAIYNFL GLSVGCIVHG LDDAQRKDQY NRDITYGTNN
     EFGFDYLRDN MKFTVEDLVQ RDYFFAIVDE VDSILIDEAR TPLIISGPGE KSSELYVQID
     RLIPRLKREE HYAVDEKSRT AALTEDGVAK CEELLRVDNL YDPRYIDLLH HIQQALKAHT
     LFKLDVDYIV KDGEVIIVDE FTGRLMPGRR FSEGLHQALE AKENVKVASE NQTLATITFQ
     NYFRMYEKLS GMTGTADTEA EEFRKIYNLD VVVIPTHRPM VRKDNPDQIY RTEREKFDAV
     VREIKDLHAK GRPVLVGTIN IDKSEQLSKM LKRQGVPHHV LNAKHHAQEA EIVAAAGQKN
     AVTISTNMAG RGTDIVLGEG VPELGGLHIL GTERHESRRI DNQLRGRAGR QGDPGSSRFY
     VSLEDDLMRL FGSERISGIM TKLGMEEGEP IEHNLISKAI ENAQRKVEGR NFEIREQLLK
     YDDVLNKQRE VVYAQRRQAL TGEGVHEAVA EMIEEQAHQL AEAHADEKIP LEQRDAQALA
     EAVFNVFGFK PELPEPAQWD AQTLAEEIIA RARAVYQRKF DEYGAPIMLQ VEQWVLLDTV
     DAHWKDHLLN MDHLKEGIGL RGYAQKDPLR EYQREGFEMF SAMAQSVQME TVAKLMRVQL
     SRPEDAVQLA PQDDTPLSYS GPDAGAPEPV RRSAKKVGRN DPCPCGSGKK YKKCCGAKG
//
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