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Database: UniProt
Entry: A4ETB1_9RHOB
LinkDB: A4ETB1_9RHOB
Original site: A4ETB1_9RHOB 
ID   A4ETB1_9RHOB            Unreviewed;       899 AA.
AC   A4ETB1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 93.
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   ECO:0000313|EMBL:EBA16950.1};
GN   ORFNames=RSK20926_08272 {ECO:0000313|EMBL:EBA16950.1};
OS   Roseobacter sp. SK209-2-6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA16950.1, ECO:0000313|Proteomes:UP000005964};
RN   [1] {ECO:0000313|EMBL:EBA16950.1, ECO:0000313|Proteomes:UP000005964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA16950.1,
RC   ECO:0000313|Proteomes:UP000005964};
RA   Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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 both as a receptor for the
CC       preprotein-SecB complex and as an ATP-driven molecular motor driving
CC       the stepwise translocation of polypeptide chains across the membrane.
CC       {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-YajC and YidC. {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, ECO:0000256|RuleBase:RU003874}.
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:EBA16950.1}.
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DR   EMBL; AAYC01000004; EBA16950.1; -; Genomic_DNA.
DR   RefSeq; WP_008205598.1; NZ_AAYC01000004.1.
DR   AlphaFoldDB; A4ETB1; -.
DR   eggNOG; COG0653; Bacteria.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000005964; 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; 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; 2.
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; 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; 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|ARBA:ARBA00022519};
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:UP000005964};
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          5..614
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          91..249
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          423..622
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          844..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         107..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   899 AA;  100667 MW;  7235646E01F1B4FF CRC64;
     MLGIGTLAKK VFGTPNDRKI KATRPLVAKI NALEETFGKL SDEGLIEKTE ELRQRALGGE
     SLDILLPEAF ANVREGARRA LGLRAFDTQL MGGIFLHQGN ISEMKTGEGK TLVATFPAYL
     NALSGKGVHV VTVNEYLAKR DAEWMGKVFA ALGMTTGVIW AGQPDDEKMA AYQSDITYAT
     NNELGFDYLR DNMKPSLDQV FQKQHNFAIV DEVDSILIDE ARTPLIISGP AEDRSELYVA
     IDKMIPFLAE EHYEIDEKTR SVTFTEDGND FLEQKLLEQG LLQEGASLYD PESTTVVHHV
     NQALRAHKLF QRDKDYIVRD GEVMLIDEFT GRMMAGRRLS DGLHQAIEAK EEVNIQPENT
     TLASVTFQNY FRLYNTLSGM TGTALTEAEE FAEIYGLGVV EVPTNRPIAR VDEDDKVYRT
     AAEKYQAMVK ATQIAHDKGQ PVLLGTTSIE KSELLSQLLQ QAGIKHNVLN ARHHEQEAQI
     VADAGRLGAV TIATNMAGRG TDIKLGGNVE FKVMEAIAAD PEADHGELRA RIEAEHAKDE
     EAVKKAGGLY VMASERHESR RIDNQLRGRS GRQGDPGRTS FYLSLEDDLM RIFGSERLDK
     ILSSLGMKEG EAIIHPWVNK SLERAQAKVE GRNFDMRKQV LKFDDVMNDQ RKVIFGQRRE
     IMAAVEIEEI VADMRHEVID ELIDTYMPPK TYADQWDTEG LQAAVLEKLS IEAPVAEWAA
     EEGVDDEQIS ERLVAASDQM MAEKTEAFGV ENMRNIEKQV LLQTIDEKWR EHLLTLEHLR
     SVVGFRGYAQ RDPLNEYKNE SFQLFEGLLE SLREAVTQQL SRVRPMTDEE QQQMLMEMAA
     RQAAMQQAAQ QSMEPVGNPE EAADGFVEDD PSTWGNPSRN DKCPCGSGKK FKHCHGRLA
//
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