SECA_BACTN
ID SECA_BACTN Reviewed; 1106 AA.
AC Q89ZL5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=BT_4362;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AE015928; AAO79467.1; -; Genomic_DNA.
DR RefSeq; NP_813273.1; NC_004663.1.
DR RefSeq; WP_008764528.1; NC_004663.1.
DR AlphaFoldDB; Q89ZL5; -.
DR SMR; Q89ZL5; -.
DR STRING; 226186.BT_4362; -.
DR PaxDb; Q89ZL5; -.
DR PRIDE; Q89ZL5; -.
DR EnsemblBacteria; AAO79467; AAO79467; BT_4362.
DR GeneID; 60925539; -.
DR KEGG; bth:BT_4362; -.
DR PATRIC; fig|226186.12.peg.4439; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR InParanoid; Q89ZL5; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 3.
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; PTHR30612; 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..1106
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320733"
FT REGION 1021..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 193..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1090
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1106 AA; 126281 MW; 079F3342B478C982 CRC64;
MGFNEFLSSI FGNKSTRDMK EIKPWVEKIK AAYPEIEALD NDALRAKTEE LKKYIRESAT
DERAKVEELK ASIESTELED REEVFAQIDK IEKEILEKYE KALEEVLPVA FSIVKATAKR
FTENEEIVVT ATEFDRHLAA TKDFVRIEGD KAIYQNHWNA GGNDTVWNMI HYDVQLFGGV
VLHKGKIAEM ATGEGKTLVA TLPVFLNALT GNGVHVVTVN DYLAKRDSEW MGPLYMFHGL
SVDCIDRHQP NSDARRQAYL ADITFGTNNE FGFDYLRDNM AISPKDLVQR QHNYAIVDEV
DSVLIDDART PLIISGPVPK GDDQLFEQLR PLVERLVEAQ KALATKYLSE AKRLIASNDK
KEVEEGFLAL YRSHKCLPKN KALIKFLSEQ GIKAGMLKTE EIYMEQNNKR MHEVTEPLYF
VIEEKLNSVD LTDKGIDLIT GNSEDPTLFV LPDIAAQLSE LENQNLTNEQ LLEKKDELLT
NYAIKSERVH TINQLLKAYT MFEKDDEYVV IDGQVKIVDE QTGRIMEGRR YSDGLHQAIE
AKERVKVEAA TQTFATITLQ NYFRMYHKLS GMTGTAETEA GELWDIYKLD VVVIPTNRPI
ARKDMNDRVY KTKREKYKAV IEEIEKLVQA GRPVLVGTTS VEISEMLSKM LTMRKIEHSV
LNAKLHQKEA EIVAKAGFSC AVTIATNMAG RGTDIKLSPE VKAAGGLAII GTERHESRRV
DRQLRGRAGR QGDPGSSVFF VSLEDDLMRL FSSDRIASVM DKLGFQEGEM IEHKMISNSI
ERAQKKVEEN NFGIRKRLLE YDDVMNKQRT VVYTKRRHAL MGERIGMDIV NMIWDRCANA
IENNDYEGCQ MELLQTLAME TPFTEEEFRN EKKDTLAEKT FNIAMENFKR KTERLAQIAN
PVIKQVYENQ GHMYENILIP ITDGKRMYNI SCNLKAAYES ESKEVVKAFE KSILLHVIDE
AWKENLRELD ELKHSVQNAS YEQKDPLLIY KLESVTLFDA MVNKINNQTI SILMRGQIPV
QEAPADEQQP RRVEVRQAAP EQRQDMSKYR EQKQDLSDPN QQAAASQDTR EQQKREPIRA
EKTVGRNDPC PCGSGKKYKN CHGQNA
