ID A0A1V6LQB2_9FLAO Unreviewed; 1120 AA.
AC A0A1V6LQB2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 38.
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:OQD42362.1};
GN ORFNames=BUL40_11385 {ECO:0000313|EMBL:OQD42362.1};
OS Croceivirga radicis.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceivirga.
OX NCBI_TaxID=1929488 {ECO:0000313|EMBL:OQD42362.1, ECO:0000313|Proteomes:UP000191680};
RN [1] {ECO:0000313|EMBL:OQD42362.1, ECO:0000313|Proteomes:UP000191680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSG9 {ECO:0000313|EMBL:OQD42362.1,
RC ECO:0000313|Proteomes:UP000191680};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_01382}.
CC Note=Distribution is 50-50. {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:OQD42362.1}.
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DR EMBL; MTBC01000007; OQD42362.1; -; Genomic_DNA.
DR RefSeq; WP_010520088.1; NZ_AFOE01000059.1.
DR AlphaFoldDB; A0A1V6LQB2; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000191680; 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:000246; Preprotein translocase subunit SecA; 1.
DR FunFam; 3.40.50.300:FF:000694; 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; 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-like.
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; NF009536; PRK12901.1; 1.
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}; 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:UP000191680};
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..770
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 617..786
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 716..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..103
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1030..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1120 AA; 127536 MW; 9BBFB31E5E113AF6 CRC64;
MSILNSVLKI FVGDKSEKDV KAIQPLVKKI KSFEEEISRL SHDQLRQKTQ EFKALIAEKC
ASVNAQISQL QEEVENSTDI DRNEEIYAEI DKLNEEVYKI SEEVLNDILP EAFAVVKETA
KRFANNTTLT VKATEFDRSI SGRADYVTLQ GEEAVWKNSW DAAGKEVTWD MVHYDVQLIG
GIALHQGKIA EMQTGEGKTL VATLPLYLNA LSGKGAHLVT VNDYLARRDS AWMAPLFEFH
GLSVDCIDNH QPNSDSRRAA YNADITYGTN NEFGFDYLRD NMAHTPKDLV QRPHHYAIVD
EVDSVLIDDA RTPLIISGPV PEGDRHEFTE LKPKVADIVQ KQRQYLTGVL AEAKNLIKSG
DTKEGGFLLL RVHRGLPKNK ALIKFLSEEG VKQLLQKTEN FYMQDNNREM VKVDEELLFT
IDEKNNQIEL TDKGVEYLSG GQDKDFFVMP DIGAEIAQIE NQNLEIEKEA ELKDELFKEF
AVKSERIHTM SQLLKAYTLF EKDVEYVVMD NKVLIVDEQT GRIMDGRRYS DGLHQAIEAK
ENVKIEALTQ TFATITLQNY FRMYNKLSGM TGTAVTEAGE FWEIYKLDVV EIPTNRPIAR
DDRHDLIYKT KREKYNAIID EVTKLAQSGR PVLIGTTSVE ISELLSKLLS VRKVQHNVLN
AKLHKKEADI VAEAGKPGVV TIATNMAGRG TDIKLTTDVK DAGGLAIIGT ERHDSRRVDR
QLRGRSGRQG DPGSSQFYVS LEDNLMRLFG SERVAKMMDR MGLEDGEVIQ HSMMTKSIER
AQKKVEENNF GIRKRLLEYD DVMNAQREVI YKRRKHALQG DRLKVDIANM IYDTSEVISE
TNKMADDFKN FEFELIKYFS ITAPMTEAEF GKMSVQDVAL KVYDQAYKHY QDKVARSAEQ
AFPVIKNVYE NQADRFERIV VPFTDGIKTL NVVTNLKEAY ESNGKQLILD FEKNITLAII
DDSWKTHLRK MDELKQSVQL AVHEQKDPLL IYKFEAFELF KTMMDKVNKE VISFLFKGEL
PSENTNQIKE AKTVSRPKEK LQTTKEEIPN SDELAAQNRA AGQTQAQRPQ KTETITREAP
KIGRNDRVTI KNIMSGENKT LKYKQAEPLI NKGEWVLVNN
//
