ID A0A1G8C5X9_9ACTN Unreviewed; 744 AA.
AC A0A1G8C5X9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=SAMN05421505_11570 {ECO:0000313|EMBL:SDH40748.1};
OS Sinosporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sinosporangium.
OX NCBI_TaxID=504805 {ECO:0000313|EMBL:SDH40748.1, ECO:0000313|Proteomes:UP000198923};
RN [1] {ECO:0000313|EMBL:SDH40748.1, ECO:0000313|Proteomes:UP000198923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201354 {ECO:0000313|EMBL:SDH40748.1,
RC ECO:0000313|Proteomes:UP000198923};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCN01000015; SDH40748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8C5X9; -.
DR STRING; 504805.SAMN05421505_11570; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000198923; 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; 3.
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; IPR026389; SecA_Actinobact-type.
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; TIGR04221; SecA2_Mycobac; 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};
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:UP000198923};
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 1..556
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 76..235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 403..557
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 92..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 744 AA; 81047 MW; 43FAFDEDEAE44138 CRC64;
MASISDLFRR FLDRPGSVNL TPFLKVVAEA GKREERVKAL DQLPPPPAGD LAEFCAIVRE
AADRTLGLRP YDVQLTGALA LLAGHVAEMA TGEGKTLSGA IAAAGYALQG HRVHVISVND
YLARRDAEWM GPFYEALGVS VGWIGQTSTR EERREAYARQ VTYGSVSEIG FDVLRDRLST
DVADLVMTEP NVALVDEADS VLVDEARVPL VMAGATDRGG AVPQTAALVR RLVRGYHYEI
DDQARNVYLT SKGIDAVEQA LGVTDLYGDP AQITDVNLAL HAHALLTKDV DYIVRDGKVH
LINPSRGRVA LLQRWPDGLQ AAVEAKEAIP ASETGEILDS VTVQGLITRY PQVCGMTGTA
VAVGEQLREF YNLTVAVIPP NRACVRVDEE DRLFATIADK RRALVEEIAA AHALGRPILI
GTLDVAESEE LADLLRARGL ECVVLNAKND AEEASIVARA GEHGAITVST QMAGRGTDIR
LGEGVAELGG LYVIGCGRHA SSRLDDQLRG RAGRQGDPGG SAFFVALDDD LITQYAPEER
PPAPDADGVV RHRRAAYLVG HAQRVAEGVN LEIHRNTWRY TRLLEKQREL VLERREKVLR
GDSAGDGLAE AAPERWAELL DTVPEEVLQE AARAIVLYHL DRGWADHLAF LNDLREGIHL
RALGRMSPID EFHREAVPAY ATFMAEVESK ALTTFAEADI TADGLTMPGE LKRPSSTWTY
LVQDNPFGSE WDRVFKRISA SVRG
//
