ID A0A4S4HB63_9BACT Unreviewed; 1132 AA.
AC A0A4S4HB63;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=secA {ECO:0000256|HAMAP-Rule:MF_01382,
GN ECO:0000313|EMBL:THG53579.1};
GN ORFNames=E5990_04340 {ECO:0000313|EMBL:THG53579.1};
OS Muribaculaceae bacterium.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2498093 {ECO:0000313|EMBL:THG53579.1, ECO:0000313|Proteomes:UP000305401};
RN [1] {ECO:0000313|EMBL:THG53579.1, ECO:0000313|Proteomes:UP000305401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM86_A22 {ECO:0000313|EMBL:THG53579.1,
RC ECO:0000313|Proteomes:UP000305401};
RA Navarre W., Wong E., Huang K.C., Tropini C., Ng K., Yu B.;
RT "Microbes associate with the intestines of laboratory mice.";
RL Submitted (APR-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}.
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:THG53579.1}.
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DR EMBL; SSTG01000034; THG53579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S4HB63; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000305401; 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; 3.10.450.50; -; 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; 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 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; 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 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};
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 4..774
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 178..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 606..790
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1030..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 194..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1132 AA; 128170 MW; E5FE92FB85C2ADB1 CRC64;
MSVLSILNKL FGNKSQRDLR EIQPIVDQIN ALGPDMKKLS NDELRQIVTD VKKQLADAVS
DDSQAIADIK SRIEDLPFEE RQPLWDEIDK REKNILDTYE RELDKALPNV FAAMRETASR
FASNATIEVT ATQMDRDLAA SGKDFVSIEG DKAIYNNHWL AGGNEIVWDM VHYDVQLIGG
IVLHQGKIAE MATGEGKTLV ATLPVFLRSL TGRGVHVVTV NDYLSKRDSE WMGPLYMFHG
QSVDCIDKHQ PNSSERRAAY MCDITFGTNN EFGFDYLRDN MAMAPSDMVQ RKHYYAIVDE
VDSVLIDDAR TPLIISGPVP KGDDQMFNDF KHNVERVYDA QRRLAGKLLM EAKEKIASDD
KDVRKEGALA LFRAYKGLPK NSSLIKYLSQ EGIKPLLLET EAYYLQDNSR EMPKATEPLY
FVIDEKNRSV ELTDKGIDEL TGHSADPQFF VLPDIASQLS EVEGDESLTP EQRQEKKDAL
LDNYSIKAER VHTVTQLLKA YTLFEKDVEY VIDDNKIKIV DEQTGRIMEG RRYSDGLHQA
IEAKEGVKVE AATQTFATIT LQNYFRMYHK LAGMTGTAET EAGEFWDIYK LDVVTIPTNK
PVARIDMDDR LFKTKKEKYA AVIEHIVELV GQGRPVLVGT TSVEISELLS KMLTLRHIPH
NVLNAKLHQK EADIVAQAGK KSTVTIATNM AGRGTDIKLS AEVKAAGGLA IIGTERHESR
RVDRQLRGRS GRQGDPGSSV FYLSFEDQLM RLFASDKVAK MLDRMGIKEG EMIESKMLNH
SIETAQKRVE ENNFGIRKRL LEYDDVMNKQ RQYIYSRRQH ALVGERIGID INNMLYDTVE
NIVNVYDSPT DYPELKMEIL KVFSVEVPFS EEEFPKMSRQ DVLNAITKAV YDGFERKSER
IVEITYPVIK DAVENHDAKG RILVPITDGK RIFNIPADVQ DAYNTHCKSI VKEWHKAIML
VTIDEVWKEH LRELDQLRQS VQNASYEQKD PLVIYKVESF HLFENAMNTL NVKAVSALMR
GQIYIPEQPR QPVAPRAAEA QLESEKGVSE SQRRMPEMRK AMPERPNDYS RYRTSRESAG
LPGEAEQRAA ASAPQGQQTH SQPIVNGPKV GRNDPCPCGS GKKFKNCHGK GL
//
