ID A0A2N3HP43_9FLAO Unreviewed; 1117 AA.
AC A0A2N3HP43;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 31.
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:PKQ46697.1};
GN ORFNames=CSW08_01475 {ECO:0000313|EMBL:PKQ46697.1};
OS Confluentibacter flavum.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Confluentibacter.
OX NCBI_TaxID=1909700 {ECO:0000313|EMBL:PKQ46697.1, ECO:0000313|Proteomes:UP000233435};
RN [1] {ECO:0000313|EMBL:PKQ46697.1, ECO:0000313|Proteomes:UP000233435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3B {ECO:0000313|EMBL:PKQ46697.1,
RC ECO:0000313|Proteomes:UP000233435};
RA Yu L.;
RT "Confluentibacter flavum sp. nov., isolated from the saline lake.";
RL Submitted (DEC-2017) 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:PKQ46697.1}.
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DR EMBL; PJEO01000009; PKQ46697.1; -; Genomic_DNA.
DR RefSeq; WP_106658138.1; NZ_PJEO01000009.1.
DR AlphaFoldDB; A0A2N3HP43; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000233435; 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; 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; 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};
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:UP000233435};
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 602..786
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 692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1117 AA; 127046 MW; 95B4D1271F27577D CRC64;
MSFLNAVLKA FVGDKSKQDV KAITPLVDKI KTFEKAMEAL SHDELRAKTA EFKAKIADAN
KDNNEQIAKL LVEAENTEDI DKREDIYQDI DKLKDDAYTI TEDVLNAILP EAFAVVKETA
KRFKNNTTLT VTANTFDREI SGAKDYVTLD NDKAIWSNSW DAAGKPITWD MVHYDVQLIG
GIALHQGKIA EMQTGEGKTL VATLPMYLNA LSGKGVHLVT VNDYLAKRDS AWMAPIFQFH
GLTVDCIDYH QPNSEARIKA YNADITYGTN NEFGFDYLRD NMAHAPNDLV QRPHHYAIVD
EVDSVLVDDA RTPLIISGPI PQGERHEFNE LKPKVDDIVA VQRKYLTGVL AEAKKLIAAG
DTKEGGFQLL RVYRGMPKNK ALIKFLSEEG IKQLLQKTEN SYMQDNNREM PKVDAELYYV
IEEKNNQIEL TDKGVEYISG ADNPTFFIMP EIGIEIAKIE NQNLSKEEEA KLKEELFKDF
GIKSERIHTL NQLLKAYALF EKDIQYVVID NKVMIVDEQT GRIMDGRRYS DGLHQAIEAK
ENVKIEDATQ TFATVTLQNY FRMYRKLSGM TGTAVTEAGE FWEIYKLDVV EIPTNRPVSR
DDRDDLVYKT KREKYNAVID EVTQLSQAGR PILIGTTSVE ISELLGKMLT IRKIPHNVLN
AKLHKKEADI VAEAGQSGQV TIATNMAGRG TDIKLSDAVK KAGGLAIIGT ERHDSRRVDR
QLRGRAGRQG DPGSSQFYVS LEDNLMRLFG SERIAKMMDR MGLKEGEVIQ HSMISKSIER
AQKKVEENNF GVRKRLLEYD DVMNAQREVV YKRRRHALHG ERLRVDLANM IFDITENISE
TNKAANDFKN FEFELIRYFS MGSPITEAEF GKLSAQEITS KVYKDAFNHY RDKMTRNADM
AFPVIKNVYE TQRDKFKRIV VPFTDGVKSL SVVTDLEKAY QTGGKQLITD FEKNITLAII
DDAWKTHLRK MDELKQSVQL AVHEQKDPLL IYKFEAFELF KSMIDEVNKD VISFLFKGEL
PSETQNTIQE AKVRRQEKLN VQKDEIPNLD ERSVQSRAAG NTQRQPHVVE TIVRERPKIG
RNDQVTIKQV ITGENKTLKY KQAEPLLAKG DWVLVED
//
