SECA_PORG3
ID SECA_PORG3 Reviewed; 1113 AA.
AC B2RKT2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=PGN_1458;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG33977.1; -; Genomic_DNA.
DR RefSeq; WP_012458284.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RKT2; -.
DR SMR; B2RKT2; -.
DR STRING; 431947.PGN_1458; -.
DR PRIDE; B2RKT2; -.
DR EnsemblBacteria; BAG33977; BAG33977; PGN_1458.
DR GeneID; 29256642; -.
DR KEGG; pgn:PGN_1458; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; PGIN431947:G1G2V-1660-MON; -.
DR Proteomes; UP000008842; 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: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 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 TIGRFAMs; TIGR00963; secA; 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; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..1113
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145042"
FT REGION 1042..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1067
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 1097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1099
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1113 AA; 127241 MW; C233BBDD5F803C52 CRC64;
MGFNEFMSKL FGNKSQRDLK EVKPFVDKIK VAYGEIERLS DDDLRGRTAI LRQKIQDYVK
DERAEIDKLK VEVEGKDLDE REEIWAKVDK LEKEILDKME VVLDEILPEA FAIIKDTARR
FAQNETIRVK ATDLDRDLAI NHDFVSIEGD TAVYQNHWVA GGNEILWDMI HYDVQLIGGT
VLHKGKIAEM ATGEGKTLVA TLPVFLNALT GNGVHVVTVN DYLSKRDSEW MGPLYMFHGL
TVDCIDKHQP NSDARRKAYN ADITFGTNNE FGFDYLRDNM ATSPKDLVQR KHNYAIVDEV
DSVLIDDART PLIISGPTPK GEDQLFEEFL PNVEKVVEAQ RKLCSQLLID AKNKMASEDK
KEQEEGSLLL YRSFKGLPKN KQLIKYLSEP GIKSSMLKTE EAYMAENMRN MHLVTDELYF
IIDEKRNSVE LTEKGIDLLT SRTDDPKFFV LPDIAAELSA LDNMESDAEK RREAKDEIIA
NYSIKSERVH TVNQLLKAYA LFEKDDQYVV MDNKVLIVDE QTGRIMDGRR YSDGLHQAIE
AKEHVKVEAA TQTFATITLQ NYFRMYHKLA GMTGTAETEA GELWDIYKLD VVVIPTNKPI
ARKDMNDRIY KTAREKYAAV IEEIVRLVEE GRPVLVGTTS VEISELLSRM LRLRGIQHNV
LNAKLHQKEA EIVAQAGQKG TVTIATNMAG RGTDIKLSAE VKKAGGLAII GTERHESRRV
DRQLRGRSGR QGDPGSSIFY VSLEDHLMRL FATEKIASLM DRLGFKEGEV LENNMLSKSV
ERAQKKVEEN NFGIRKHLLE YDDVMNSQRE VIYTRRRHAL MGERIGMDVL NTIYDVCKAL
IDNYAEANDF EGFKEDLMRA LAIESPITQE IFRGKKAEEL TDMLFDEAYK SFQRKMDLIA
EVAHPVVHQV FETQAAVYER ILIPITDGKR VYNIGCNLRE ADETRGKSII KEFEKAIVLH
TIDESWKEHL REMDELRNSV QNASYENKDP LLIYKLESYE LFRKMVEAMN RKTVAILMRA
RIPVPEAPSQ EELEHRRQIE IRHAAEQRTD MSKYRTQKDD IEAQQKAQRD AASRPQGAAA
PQTPIRNENK IGRNDPCPCG SGKKFKQCHG RNL
