ID A0A0A6Y3C7_9FLAO Unreviewed; 1118 AA.
AC A0A0A6Y3C7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HMPREF9074_07942 {ECO:0000313|EMBL:KHE70092.1};
OS Capnocytophaga sp. oral taxon 329 str. F0087.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE70092.1, ECO:0000313|Proteomes:UP000030579};
RN [1] {ECO:0000313|EMBL:KHE70092.1, ECO:0000313|Proteomes:UP000030579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0087 {ECO:0000313|EMBL:KHE70092.1,
RC ECO:0000313|Proteomes:UP000030579};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2014) 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}.
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DR EMBL; KN389995; KHE70092.1; -; Genomic_DNA.
DR RefSeq; WP_009392552.1; NZ_KN389995.1.
DR AlphaFoldDB; A0A0A6Y3C7; -.
DR STRING; 706436.HMPREF9074_07942; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000030579; 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; 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 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};
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 5..771
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 179..338
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 603..787
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1118 AA; 127540 MW; BD18D9DD31E715F9 CRC64;
MSIINSLIKL FVGDKAKNDL KSIQPLVEKI KAYAAELEHI SNDELRGKTI AFKEKIKEAR
ATFDTRIADL QTQANATEDI DKKEDLYTEI DKLSAEAYQA SEKVLNDILP EAFATMKETA
RRFATNETIS VTATPRDREL SATHDYVTIE GDKAIWKNHW DAAGKDVTWD MVHYDVQLIG
GIALHQGKIA EMQTGEGKTL VATLPVYLNA LTGNGVHLVT VNDYLARRDS AWMGPLFEFH
GLRVDCIDNH QPNSQARRNA YNADITYGTN NEFGFDYLRD NMAHTSEDLV QRAHNYAIVD
EVDSVLIDDA RTPLIISGPT PKGDRHEFNE LKPLVADLVE KQRTYLTKVL ADARKLIAEG
NTKEGGFQLL RVYRGLPKNK ALIKFLSEEG VKQLLQKTEN YYMQDNNREM PKVDAELYFV
IDEKNNQIEL TDKGFADIAS YDGDKNFFVL PDIGVEIANI ESQNLPIEEE AKLKEKLLQD
FTVKSERIHT LNQLLKAYTL FEKDVEYVLI DNKVLIVDEQ TGRIMDGRRY SDGLHQAIEA
KENVKIEAAT QTYATITLQN YFRMYSKLSG MTGTAITEAG EFWEIYKLDV MEIPTNRPIA
RKDYNDLIYK TKREKYNAVI DKVVSLSEAG RPVLIGTTSV EVSELLSRML TMRKIKHNVL
NAKLHKKEAE IVAEAGQSGV VTIATNMAGR GTDIKLSPEV KAAGGLAIIG TERHDSRRVD
RQLRGRSGRQ GDPGSSLFYV SLEDNLMRLF GSERIARLMD KLGHKEGDVI EHSIMTKRIE
TAQKKVEENN FGIRKRLLEY DDVMNAQREV IYKRRRHALE GERLKVDLAN MIFDTCEVIV
ESNKSANNYK NFEFELIKYF SLKTQISETE FAKTANNELT FRLYREVLDH YQQKTERSAA
QAFPVIREVY ENPSNTYERI VVPFTDGQKM LNIVTDLKEA YESGGKKLIS DFEKNITLAI
IDDEWKTHLR QMDELKQSVQ LAVHEQKDPL LIYKFEAFQL FKAMIDKVNK DIVSFLFRAE
LPTQAPAVQE AHAPQRSNEH YQTNKEEVLN SDEMAAQARE VGQQASQRRS VVETIIREQP
KVGRNDKVVI QNIRTGERKE LKFKQAMPLL EGDWILVN
//
