ID A0A6H9WFV4_9MICO Unreviewed; 774 AA.
AC A0A6H9WFV4;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
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=secA2 {ECO:0000313|EMBL:KAB1649782.1};
GN Synonyms=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN ORFNames=F8O04_06000 {ECO:0000313|EMBL:KAB1649782.1};
OS Pseudoclavibacter endophyticus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Pseudoclavibacter.
OX NCBI_TaxID=1778590 {ECO:0000313|EMBL:KAB1649782.1, ECO:0000313|Proteomes:UP000431744};
RN [1] {ECO:0000313|EMBL:KAB1649782.1, ECO:0000313|Proteomes:UP000431744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 60007 {ECO:0000313|EMBL:KAB1649782.1,
RC ECO:0000313|Proteomes:UP000431744};
RA Li Y.;
RT "Phylogeny of genus Pseudoclavibacter and closely related genus.";
RL Submitted (SEP-2019) 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. 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:KAB1649782.1}.
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DR EMBL; WBJY01000001; KAB1649782.1; -; Genomic_DNA.
DR RefSeq; WP_158028367.1; NZ_BMHG01000001.1.
DR AlphaFoldDB; A0A6H9WFV4; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000431744; Unassembled WGS sequence.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IEA:TreeGrafter.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
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 GO; GO:0043952; P:protein transport by the Sec complex; IEA:TreeGrafter.
DR CDD; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR FunFam; 3.40.50.300:FF:000429; Preprotein translocase subunit 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-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR026389; SecA_Actinobact-type.
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; 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:UP000431744};
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..591
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 90..251
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 417..598
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 106..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 774 AA; 84550 MW; 2972CB792BA6E81B CRC64;
MTRRVPRWLA RIAGLPGTTP FRRVEVLAGR ANDLAAEAKS LGDGELRTRA RAAAVGATAG
DDDATVRYLT IAREAANRAL GLRPFDVQLQ ACAALLGGTA VEMDTGEGKT LVGAMAAAAY
ALAGHPTHLL SVNDYLAERD AEWMRPLFEL VGLDVAWIGQ RSPRDERRAA YRADVLYAPV
SEVGFDLLRD RFASTADELV SVELDTAIVD EADAVMIDEA MVPLVLAGTS AHAPDRADDA
AELVADLDEG GDFETDAERS NAWLTDDGIE RLESQLGGIN LFEPEHAPLL TRLNLALHAR
VLVQRDVDYL VTHGRIELVN AARGRVAHHQ RWPDGLHAAV EAKEGLEPSP RSVVLDSITV
QDLVRGYQRL GGMSGTVVAV ADEFTEFYDL PSGRVERNEP CRRVDELDRV FLTAAEALDD
LVAEVVARHE TGQPVLVGTQ TVAESERLAK RLRRRNIRPR VLNAKNDADE AGIVARAGEF
GSVTVSTQMS GRGTDIVLGG ADAGDRDRVV EAGGLAVLAT SRAPSTRLDA QLRGRAGRQG
DPGMSLVITS LEANLVTENA PTHTLAEIAR RGERIPEAQR RAIVRSAQSI AEGIRTDRHR
STWQYSRAIA SQRRAVLAHR ATVKRPSAID KLGASLPAPL RSLGDARRDT LFDLSYRARL
FFLDDEWTEH LALLGEVRDG IHLRSLASQN PVEEFSMIAH REFAGFFDRV DERFREFLDA
LDPDDLDRDA TELGLRRPSS TWTYMVTDDP FGSVGGRFAR RAGGFLRSKV LKLE
//
