ID A0A347VTT7_9HELI Unreviewed; 867 AA.
AC A0A347VTT7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:TLD92030.1};
GN ORFNames=DCO61_08650 {ECO:0000313|EMBL:MWV70065.1}, LS64_010920
GN {ECO:0000313|EMBL:TLD92030.1};
OS Helicobacter saguini.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1548018 {ECO:0000313|EMBL:TLD92030.1, ECO:0000313|Proteomes:UP000029714};
RN [1] {ECO:0000313|EMBL:TLD92030.1, ECO:0000313|Proteomes:UP000029714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD92030.1,
RC ECO:0000313|Proteomes:UP000029714};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:TLD92030.1, ECO:0000313|Proteomes:UP000029714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD92030.1,
RC ECO:0000313|Proteomes:UP000029714};
RX PubMed=27245408; DOI=.1128/IAI.00235-16;
RA Shen Z., Mannion A., Whary M.T., Muthupalani S., Sheh A., Feng Y., Gong G.,
RA Vandamme P., Holcombe H.R., Paster B.J., Fox J.G.;
RT "Helicobacter saguini, a Novel Helicobacter Isolated from Cotton-Top
RT Tamarins with Ulcerative Colitis, Has Proinflammatory Properties and
RT Induces Typhlocolitis and Dysplasia in Gnotobiotic IL-10-/- Mice.";
RL Infect. Immun. 84:2307-2316(2016).
RN [3] {ECO:0000313|EMBL:TLD92030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD92030.1};
RA Sheh A., Shen Z., Mannion A.J., Fox J.G.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MWV70065.1, ECO:0000313|Proteomes:UP000477070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-048 {ECO:0000313|EMBL:MWV70065.1}, and 16-048 (F4)
RC {ECO:0000313|Proteomes:UP000477070};
RA Mannion A., Shen Z., Fox J.G.;
RT "Multi-Generational Helicobacter saguini Isolates.";
RL Submitted (DEC-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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:TLD92030.1}.
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DR EMBL; QBIU01000001; MWV70065.1; -; Genomic_DNA.
DR EMBL; JRMP02000024; TLD92030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347VTT7; -.
DR STRING; 1548018.LS64_12835; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000029714; Unassembled WGS sequence.
DR Proteomes; UP000477070; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004027; SEC_C_motif.
DR InterPro; IPR000185; SecA.
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; PF02810; SEC-C; 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; SM00490; HELICc; 1.
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}; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000029714};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..587
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 103..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 419..603
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 803..830
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 119..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 867 AA; 98747 MW; 2CA5B933DB3375C8 CRC64;
MTAIMGKIFG TKNDKVLKQY RNRVARINAM EFDLEKKSDL DLQNRMNEIK DEIAKKMESL
DSKELGLEIL NTLLDNNLEE VFALTREASK RVLNMRHFDV QLIGGMALHD GKIAEMKTGE
GKTLVATLPV ILNALSGKSV HVVTVNDYLA RRDSNTMAPL YNFFGFSVGV VTSGLQDDVE
RLNIYSNNIV YGTNNEYGFD YLRDNMKYNL EQKVQKHHFF AIIDEVDSIL IDEARTPLII
SGPVNKKMEN YQIADSVAKA LKSPQDFTID EKNRVILTTE DGIKKAEKLF KVENLYAIEN
ASLSHHLDQA LKANYLFVKD KDYVVQNGEV VIVDEFTGRL SEGRRFSEGL HQALEAKEGV
NIKEESQTLA DITFQNYFRL YDKLGGMTGT AQTEATEFLE IYKLEVVSIP TNLPVARKDL
NDLIYKSEIE KFNAVINKIV ELHKIGQPVL VGTASIEKSE KLHELLKKAR IPHNVLNAKQ
HEKEAEIIKN AGLKGAVTIA TNMAGRGVDI KIDDEVKALG GLYIIGTERH ESRRIDNQLR
GRAGRQGDPG TSQFYLSLED SLLRIFGSDR LKGIMGKLGL KDGESIESSM ITKSVEKAQK
KVESMHFESR KHLLEYDDVS NEQRKVIYRF RNELLQKDFE MQERIDENRI LSVQSLLEKH
DIMPHDVSEN YNLESLCAGL KEEYLLELDS KALAGKTYDE ISEVIIESLA AKYDEKFSHT
DSKMRNELER IIYLQVVDNA WREHLYSIDH LKTGISLRGY NQKDPLVEYK KESYNLFLEL
IENIKIEAYR TLQIIQFASQ DVSREEDKIL NELESENENL VLNYANLEDE IADKKPARND
MCPCGSGKKY KNCHGKSGPK RGMLAKN
//
