ID   A0A3N2KW29_9BACT        Unreviewed;      1144 AA.
AC   A0A3N2KW29;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   12-OCT-2022, entry version 16.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382,
GN   ECO:0000313|EMBL:ROS89781.1};
GN   ORFNames=EEL39_02955 {ECO:0000313|EMBL:ROS89781.1};
OS   Muribaculaceae bacterium Isolate-080 (Janvier).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486468 {ECO:0000313|EMBL:ROS89781.1, ECO:0000313|Proteomes:UP000277934};
RN   [1] {ECO:0000313|EMBL:ROS89781.1, ECO:0000313|Proteomes:UP000277934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-080 (Janvier) {ECO:0000313|Proteomes:UP000277934};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-2018) 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: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 membrane {ECO:0000256|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC       {ECO:0000256|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC       ECO:0000256|HAMAP-Rule:MF_01382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROS89781.1}.
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DR   EMBL; RIBG01000002; ROS89781.1; -; Genomic_DNA.
DR   EnsemblBacteria; ROS89781; ROS89781; EEL39_02955.
DR   Proteomes; UP000277934; Unassembled WGS sequence.
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; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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   PANTHER; PTHR30612; PTHR30612; 1.
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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 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};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01382}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000277934};
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          4..772
FT                   /note="SECA_MOTOR_DEAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          178..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          604..788
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1024..1144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          41..72
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1083..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         194..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1144 AA;  130235 MW;  DF8AC56B51440919 CRC64;
     MSFQSFLTKI FGNKSTRDLK EIEPIVKKIE ALEPEVKQLT IDQLRERIDN VRADISQAIS
     AEKEENERLR IEVEELPFDQ RQPVWDKIDR NEKTMLDTIE DKLNEHLPEV FAVVRETAAR
     FAANETIVVK ATQLDRELAA QGRDFVSIDG DNAIWKNHWL AGGNEMKWDM IHYRVQLIGG
     IVLHQGKIAE MATGEGKTLV ATLPVFLRSL SGRGVHVVTV NDYLSKRDSE WMGPLYMFHG
     STVDCIDKHQ PNTAARRAAY NCDITFGTNN EFGFDYLRDN MAMSPADMVQ RKHYYAIVDE
     VDSVLIDDAR TPLIISGPVP KGDDQLFDEY RPNVEKVVEA QRKLVTKILA EAKTKIASDD
     KETKKEGALL LYRAFKGLPK NGALIKFLSQ EGMKNLMLET EAYYLQDNKR EMPKVTDPLY
     FVIDEKNRSV ELTDKGIDEL TGKTGDPQFF VLPDIASQLS ETEHIENLAE RQQRKDELMQ
     DYAVKAERVH TVTQLLKAYT LFEKDVEYVI DEGKIKIVDE QTGRIMEGRR YSDGLHQAIE
     AKEHVKVEAA TQTFATITLQ NYFRMYHKLA GMTGTAETEA GEFWDIYRLD VVTIPTNRPI
     ARIDMNDRVY KTKKEKYAAV IDEIQDLVSK GRPVLVGTTS VEISELLSRM LTMRHIPHNV
     LNAKLHQKEA EIVAHAGRKG MVTIATNMAG RGTDIKLTPE VKEAGGLAII GTERHESRRV
     DRQLRGRSGR QGDPGSSVFY VSFEDQLMRL FATDRVMKML DTLGLEEGER IESSMVTNAI
     GNAQKRVEEN NFGIRKRLLE YDDVMNKQRT YIYNRRHHAL LGERIGIDIA NMIWDVIENF
     VNNYGPADYQ DLALELFRVL TIEAPFTEEE YRNMSKEDAV EKIHTAAQEA FDRKSQRILE
     VAQPVIVDCV ENRGFKGRIA VPMTDGKRFF NLVVDIDEAY RTGCKSIVKE WHKAVLLVTI
     DELWKEHLRE LDQLRQSVQN ASYEQKDPLV IYKVESFHLF EAMLNNLNVK TMSTLMRGQI
     YVQQAPPQPS RPQQPATEPE TVETGEDGAE AANNPVKQPE PQQQEAPKPQ PKVERAMPER
     PNDYSKYQTS RENLPGENAQ RAAAQGASQQ QVTQPVKSGP RINRNDPCPC GSGKKYKNCH
     GKGL
//