ID R7J2K6_9BACT Unreviewed; 1124 AA.
AC R7J2K6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=BN799_00108 {ECO:0000313|EMBL:CDE58006.1};
OS Prevotella sp. CAG:873.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262936 {ECO:0000313|EMBL:CDE58006.1, ECO:0000313|Proteomes:UP000018078};
RN [1] {ECO:0000313|EMBL:CDE58006.1, ECO:0000313|Proteomes:UP000018078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:873 {ECO:0000313|Proteomes:UP000018078};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE58006.1}.
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DR EMBL; CBJF010000185; CDE58006.1; -; Genomic_DNA.
DR AlphaFoldDB; R7J2K6; -.
DR Proteomes; UP000018078; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018078};
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..772
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 620..788
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1023..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1067
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 694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1124 AA; 127731 MW; 7BD0DF982309F3B9 CRC64;
MSFTGFLSKI FGDKSSRDRK LLQPLVDRIN AIGPDLKPLT NDELRARIDA VRADIDGATA
EDRKAIEEAR ATIETLPVDQ RQHLWDEIDR REKNILDTLE KKLDEHLCEV FAVMRETAAR
FAANADVVVT ARQLDRDLAA QGRDFVTIDG DKAIWHNHWM AGGNEITWDM VHYDVQLMGG
IVLHQGKIAE MATGEGKTLV ATLPVFLRSL SRRGVHVVTV NDYLSKRDSE WMGPLYMFHG
STVDCIDKHE PNTPERRAAY NCDITFGTNN EFGFDYLRDN MAMDPEDMVQ RKHYYAIVDE
VDSVLIDDAR TPLIISGPVP KGDDQYFDEF KQNVKNVVQA QQRLVTQILA EAKAKLVSED
KDTRKEGALL LFRAFKGLPK NGALIKFLST EGMKNILLET EAHYLQDNAR EMPIVTDPLY
FVIDEKNRSV ELTDKGIDEL TRGISDPQFF VLPDITAQLS DLEHITNPEE RAERKDTLMQ
DYAVKAERVH TVTQLLKAYT LFEKDVEYVI DDGKIKIVDE QTGRIMEGRR YSDGLHQAIE
AKEGVKVEAA TQTFATITLQ NYFRMYHKLA GMTGTAETEA GEFWDIYKLD VVTIPTNKPV
ARIDMNDRVY RTKREKYAAV IDEIVRLVGE GRPVLVGTTS VEISELLSRM LQMRRIPHNV
LNAKLHQKEA EIVAQAGRKG TVTIATNMAG RGTDIKLTPE VKAAGGLAII GTERHESRRV
DRQLRGRAGR QGDPGTSVFY VSFEDQLMRV YANDRIMKLL DTFGFKEGEM LEHKMINNSI
EKAQKRVEEN NFGIRKHLLE YDDVMNKQRT YIYTRRHHAL VGERIGIDIS NMIYDAIENL
VSNYEQAADF DDLTVELMRV LTIEPPFTAE EYANLEKEDR IERLHAAAIE TLDRKSQRIR
EIVMPVVKAS VEEGQTGIRA IPITDGKRIF RILFDIEEAN RTDGASLVKE WQKKLLLLTI
DELWKEHLRE LDDLRQSVRN ASYEQKDPLV IYKVESFHMF ERMLANLNAK AVSTLMRGQV
YIPEPRPQQE QPSAPEMSRA MPQQRAPRPN YRTSRGDFKT ASATLPSEAN AAAAAEAAQR
AAAAQRQNEP QRTMPVKAGP RIGRNDPCPC GSGKKYKNCH GRNQ
//
