ID A0A2T6DB00_9BACT Unreviewed; 973 AA.
AC A0A2T6DB00;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PTX99617.1};
GN ORFNames=DB346_17455 {ECO:0000313|EMBL:PTX99617.1};
OS Verrucomicrobia bacterium LW23.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=2161867 {ECO:0000313|EMBL:PTX99617.1, ECO:0000313|Proteomes:UP000244158};
RN [1] {ECO:0000313|EMBL:PTX99617.1, ECO:0000313|Proteomes:UP000244158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW23 {ECO:0000313|EMBL:PTX99617.1,
RC ECO:0000313|Proteomes:UP000244158};
RA Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT "Genomic and phenotypic characterization of four novel plant-associated
RT Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL Submitted (MAR-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 -!- 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, 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:PTX99617.1}.
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DR EMBL; QAZA01000045; PTX99617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6DB00; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000244158; 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; 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; 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; 2.
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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000244158};
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 3..696
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 104..262
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 542..712
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 932..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 391..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 936..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 120..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 973 AA; 110356 MW; 592587BADDADD8C1 CRC64;
MLSWVLKKIL GTKNERELAR IRPIVAKINA IEQDLQQVSD ATLIAKTAEM KERYQKGETL
DQLLPEAFAV VKNCARRFAA AKRQVEVRGQ MMTWEMVHFD VQLIGGMVLH GGRIAEMGTG
EGKTLVATLP VYLNALTGKG VHVITVNDYL ASRDAEWMGE IYRFLGLTVG CIQRDQSPDV
RRQMYQCDIT YGTNSEFGFD YLRDNGMATT REDQVQRGHA YAIVDEVDSI LIDEARVPLI
IAGPVSVSSH QYDKFKPVIE RLVQAQTVEC NRWANEAKRL IDSKGDMEEA GRLLYKVKLS
MPQHRILARI IEDGVARRAM DDAELVLYQD PRRIDYFKLR EEAYFSIDVK SHDADLTERG
REYLNPNDPK MFLIPDIATE FHEIEAKGGT AEEKARRKQE AQVNYDDASE RIHNISQLLK
AYCIMEKDRQ YVVQDNKVVI VDEFTGRPMP GRRWSDGLHQ AVEAKEGVQI DRETQTMATI
TIQNYFRLYE KLAGMTGTAE TEANEFKDIY KLEVIVIPPN RKISRVDHND SIYKTRRAKY
NAIIQEIKAA HEHGQPVLVG TVAVDSSEVL SRMLKREGIP HTVLNARYHQ QEAEIVARAG
QKGAVTIATN MAGRGTDIKL GPGVHELGGL YVIGTERHEA RRIDRQLRGR CARQGDPGVS
KFYVSFEDDL MTNFGDSRRI SGIMTALGMT DDEELEHPWL NKSVESAQKR VEQRNYSVRR
YTLQYDDVMN QQRMVIYEWR NAILDTETPR TEVFEAIEKV VGDECSALLT GASADPEEFL
QWVNTTFPLG LEKGDLPFDQ GSDAVEKAVL QKITEAYELK IKFEQAEAIK HIERSIVLTA
IDKLWQEHLY AMDQLRTGIS LYQHAQKDPL IEYKKEAFKM FEQLMGTINA EIVNNSFRSA
SSLEAIENFL HSLPTKMVHD LSGSGLEFTL PLPGDFPGQE LPPQSTPPAE EPKPSQGGGQ
HHGGGQHKKK KRR
//
