ID   A0A372DVV1_9BACT        Unreviewed;      1134 AA.
AC   A0A372DVV1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   19-JAN-2022, entry version 9.
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:RFP63710.1};
GN   ORFNames=D0N36_18060 {ECO:0000313|EMBL:RFP63710.1};
OS   Hymenobacter sp. CCM 8763.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=2303334 {ECO:0000313|EMBL:RFP63710.1, ECO:0000313|Proteomes:UP000262520};
RN   [1] {ECO:0000313|EMBL:RFP63710.1, ECO:0000313|Proteomes:UP000262520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8763 {ECO:0000313|EMBL:RFP63710.1,
RC   ECO:0000313|Proteomes:UP000262520};
RA   Sedlacek I., Holochova P., Kralova S., Pantucek R., Stankova E.,
RA   Vrbovska V., Kristofova L., Svec P., Busse H.-J.;
RT   "Hymenobacter humicola sp. nov., isolated from soils in Antarctica.";
RL   Submitted (AUG-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 + H(2)O + cellular protein(Side 1) = ADP + phosphate +
CC         cellular protein(Side 2).; EC=7.4.2.8; Evidence={ECO:0000256|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: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:RFP63710.1}.
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DR   EMBL; QVLT01000041; RFP63710.1; -; Genomic_DNA.
DR   EnsemblBacteria; RFP63710; RFP63710; D0N36_18060.
DR   Proteomes; UP000262520; 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: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; 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   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   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};
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}.
FT   DOMAIN          6..779
FT                   /note="SECA_MOTOR_DEAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          181..340
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          619..795
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   NP_BIND         197..201
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   COILED          85..105
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          617..637
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         701
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1134 AA;  128448 MW;  EDBDC8683FEACD57 CRC64;
     MLDFLGKTVA KLFGSKADKD LKEIVPYVAL INAEYAKLAP ISDDELRART DEVRARINAH
     LKTTDDQLAG LHERVNAEGL DALQKEDLFD QIDALEKQRN KELEVVLLEV LPLSFAITKE
     TARRYAENKQ LVVTATDYDR EYASRKGNVT IVGDQAIWSN TWLAAGAEIT WDMVHYDVQL
     IGGVVLHQGK IAEMATGEGK TLVSTLPSFL NALAKRGVHL VTVNDYLAKR DSEWNAPLFE
     FHGITVDCID KHQPNTDARR KAYLADITYG TNNEFGFDYL RDNMARDPQE LVQRKHHYAM
     VDEVDSVLID DARTPLIISG PIPRGDVHEF HQLKPRIQKV VDAQKKLVQN YLVEARKLIK
     ENNVGPKEGE GGLALFRAFR GLPKSKPLIK FLSETGMRAA LQKVENYYLQ DNSRQMPQAD
     LPLYFTIDEK NNQIELTEKG LDLITGEGED PRLFIMPDIG SEIADIEKNA ALSGEEKLHA
     KEQLMDNFQQ QSERVHTISQ LLKAYTLFER DDQYILTEDG KVKIVDEQTG RVMEGRRYSD
     GLHQALEAKE NVRVEELTQT YATVTLQNFF RMYHKLGGMT GTAETEAGEF WEIYKLDVVV
     VPTNRGIARK DEHDKVYKTV REKYNAVADE IQELVQAGRP VLVGTTSVEI SELVSRMLKF
     KGIPHQVLNA KQNQREAEIV AGAGFPGTVT IATNMAGRGT DIKLRETSKE SGGLAIIGTE
     RHESRRVDRQ LRGRAGRQGD PGSSQFFVSL EDNLMRLFGS DRIAKLMDRM GLEEGEVIQH
     SMITSSIERA QKKVEENNFG IRKRLLEYDD VMNAQREVVY KRRRNALHGE RLELDIWNMI
     YDVCEDIVVG HKGSNDFNDF QLAIIRIFGY DTHLTAQQLA GMTAGQLTQQ LYDEALGYYH
     SKNEFIGSNA MPLINDLLSQ NAPYENIAVP FTDGRKQIQA VANLRRAQAT QGQEVIRGME
     KVVVLSVIDE AWTKHLRAMD DLKQVVQNAV YEQKDPLLVY KFESFELFKQ MISKVNEDTI
     QFLFRADVPM QAGQDGEDEF EYFTEDELPV APPQPKLTME KEISSVSLGA GPEDLEQDGA
     MTQLLEKQQP ARSQKVANRN EKVSVQYMDG RIVRDVKFKQ VEDDLLNDRA VLID
//