SECA2_CLOD6
ID SECA2_CLOD6 Reviewed; 781 AA.
AC Q183M9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=CD630_27920;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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 -!- 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 membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {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; AM180355; CAJ69680.1; -; Genomic_DNA.
DR RefSeq; WP_011861685.1; NZ_CP010905.2.
DR RefSeq; YP_001089305.1; NC_009089.1.
DR PDB; 6SXH; X-ray; 2.30 A; A=1-781.
DR PDB; 6T4H; X-ray; 2.90 A; A=1-781.
DR PDBsum; 6SXH; -.
DR PDBsum; 6T4H; -.
DR AlphaFoldDB; Q183M9; -.
DR SMR; Q183M9; -.
DR STRING; 272563.CD630_27920; -.
DR PRIDE; Q183M9; -.
DR EnsemblBacteria; CAJ69680; CAJ69680; CD630_27920.
DR KEGG; cdf:CD630_27920; -.
DR KEGG; pdc:CDIF630_03055; -.
DR PATRIC; fig|272563.120.peg.2940; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; YWIDHID; -.
DR PhylomeDB; Q183M9; -.
DR BioCyc; PDIF272563:G12WB-2951-MON; -.
DR Proteomes; UP000001978; Chromosome.
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: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 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; 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; 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR TIGRFAMs; TIGR00963; secA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..781
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000320779"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT HELIX 14..34
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 214..218
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 410..426
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6T4H"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 494..497
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 550..555
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 578..624
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 630..648
FT /evidence="ECO:0007829|PDB:6SXH"
FT TURN 649..653
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 656..666
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 683..705
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 707..739
FT /evidence="ECO:0007829|PDB:6SXH"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:6SXH"
FT HELIX 750..778
FT /evidence="ECO:0007829|PDB:6SXH"
SQ SEQUENCE 781 AA; 89116 MW; 3F8720DF9815809D CRC64;
MSVIDSILDK ADEQEIKKLN VIVDKIDALE DSMKNLSYEE LKDMTAIFKN RLKKGETLDD
ILPEAFAVVR EVSKRKLGMR QYRVQLIGGI VIHQGKIAEM KTGEGKTLVE VAPVYLNALT
GKGVHVITVN DYLAERDKEL MSPVYESLGM TVGVIISNQD PNIRKQQYKC DITYGTNSEF
GFDYLRDNMV PDLSHKVQRE LNFAIVDEVD SILIDEARTP LIIAGDGDED LKLYELANSF
VKTVKEEDFE LDRKDKTIAL TASGISKAES FFGITNLTDI KNIELYHHIN QALRGHKLME
KDVDYVISNG EVMIVDEFTG RVMDGRRYTD GLHQAIEAKE GVEIKNESKT MATVTYQNFF
RLYEKLSGMT GTAKTEEGEF ESIYKLNVVQ IPTNRPVIRA DLHDKVFKTE EEKYSAVVEE
IIRIHKTRQP ILVGTVSVEK SEKLSKMLKK QGIKHQVLNA KQHDKEAEII SKAGKLDAIT
IATNMAGRGT DISLGAGDKE EEQEVKDLGG LYVIGTERHE SRRIDNQLRG RSGRQGDPGT
SRFFVSLEDD VIKLYGGKTI EKLMKRTSSN ENTAIESKAL TRAIERAQKG VEGKNFEIRK
NVLKYDDTIN EQRKVIYNER NKVLNDEDIQ EDIQKMVKDI IQEAGETYLI GRKRDYYGYF
KHLYSTFMPA DTLLIPGVDK KSVQEIIDST YEISKRVYDL KKMMLGIDKV AELEKTVLLK
VVDQYWIDHI DAMEQLKQYI GLKSYAQKDP FKEYALEGYD MFEALNKNIR EATVQYLYKF
N
