ID A0A2S8EXR9_9RHOB Unreviewed; 901 AA.
AC A0A2S8EXR9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=C2I36_01110 {ECO:0000313|EMBL:PQO24718.1};
OS Rhodobacteraceae bacterium WD3A24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO24718.1, ECO:0000313|Proteomes:UP000237945};
RN [1] {ECO:0000313|EMBL:PQO24718.1, ECO:0000313|Proteomes:UP000237945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD3A24 {ECO:0000313|EMBL:PQO24718.1,
RC ECO:0000313|Proteomes:UP000237945};
RA Wang S.;
RT "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL Submitted (JAN-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 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:PQO24718.1}.
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DR EMBL; PUHN01000003; PQO24718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8EXR9; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000237945; 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:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 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:UP000237945};
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..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 424..622
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 864..901
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 901 AA; 101322 MW; C9059B9BE39942B3 CRC64;
MLGFGTLTRK VLGTPNERKV KAVRPIVEKI NALEPEFRAL DDDALIAKTE EFKQRHAGGE
SLDSLLPEAF ANCREAAHRA LGLRAFDVQL IGGIFLHRGN IAEMKTGEGK TLVATFPTYL
NALTGKGVHI VTVNDYLAKR DAEWMGKVYS RLGMTTGVIY PQQPDAEKHG AYGADVTYAT
NNELGFDYLR DNMKSELSQM VQRGHHFAIV DEVDSILIDE ARTPLIISGP SQDRSDLYTS
VDRLVPEITE DHFTLDEKTR NVTYTDEGNE FIEHKLREAG LLPEDQSLYD PESTSLVHHV
TQALRAHKLF HRDQNYMVRD GEVVLVDEFT GRMMPGRRLS EGLHQAIEAK EGVAIQPENV
TLASVTFQNF FRLYEKLAGM TGTATTEAEE FREIYGLGVV EIPTNEPIAR LDEHDQVYRT
ANEKYDGILA AIEEAHAKGQ PILVGTTSIE KSELLSNMLD KAGIKHNVLN ARQHEKEAQI
IAEAGKFGAV TIATNMAGRG TDIQLGGNVE MKVIEALDEN PETDPEKLRE EIEAQVADEK
RRVIEAGGLF VLGTERHESR RIDNQLRGRA GRQGDPGRSC FFLSLEDDLM RIFGSERLDK
VLSGLGMKEG EAIVHPWVNK SLEKAQTKVE ARNFDIRRQL LKFDDVMNDQ RKVIFGQRLE
IMKADDLSEI VQDMRHQVID DLVDEYLPPK TYHDQWDAQG LYAAALEKLG IEVPVIAWAE
EDGVDQEVIR ERLYEASDKL MDEKAEQFGS DSMRTIEKQI LLQTIDSKWR DHLVTLEHLR
SVVGFRGYAQ RDPLNEYKTE AFALFETMLN ALREDVTQKL SRIRPLSPEE QERMMEQLAE
QQKAMEAPAK AGGVAQQADA PVPLREGFDE NDPDTWGNPG RNEPCPCGSG KKFKHCHGRL
G
//
