SECA_CHLAB
ID SECA_CHLAB Reviewed; 969 AA.
AC Q5L4W3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CAB894;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(2005).
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR848038; CAH64333.1; -; Genomic_DNA.
DR RefSeq; WP_011097405.1; NC_004552.2.
DR AlphaFoldDB; Q5L4W3; -.
DR SMR; Q5L4W3; -.
DR PRIDE; Q5L4W3; -.
DR EnsemblBacteria; CAH64333; CAH64333; CAB894.
DR KEGG; cab:CAB894; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001012; 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; 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 Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport.
FT CHAIN 1..969
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073468"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 117..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 969 AA; 111054 MW; 4089DA23851092F7 CRC64;
MLDFLKRFFG SSQERTLKKF QKLVDKVNLY DEMLAPLSDE ELRNKTAELK KRYQDGESLD
DMLPEAYAVV KNVCRRLTGT PVEVSGYHQN WDMVPYDVQV LGAIAMHKGF ITEMQTGEGK
TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSILR WLGLTTGVLI SGSPLEKRKD
IYRCDVVYGT ASEFGFDYLR DNSIATSVDE QVGRGFYFAI IDEVDSILID EARTPLIISG
PGEKHNPVYF ELKDKVADLV QLQRELCNQL ALEARRGLEL FLDMDILPKD KKVIEAISEF
CRSLWLVSKG MPLNRVLRRV REHPDLRAMI DKWDTYYHAE QNKEESIEKL SQLYIIVDEH
NNDFELTDRG MQQWVDKAGG SAEDFVMMDM GHEYALIDGD DTLSPTEKIN RKIAISEEDT
RRKARAHGLR QLLRAHLLME RDVDYIVRND QIVIIDEHTG RPQPGRRFSE GLHQAIEAKE
HVTIRKESQT FATVTLQNFF RLYEKLAGMT GTAITESKEF KEIYNLYVLQ VPTFKECLRV
DHNDEFYMTE REKYHAIVKE IARIHAVGNP ILIGTESVEV SEKLSRILRQ NRIEHTVLNA
KNHAQEAEII AAAGKLGAVT VATNMAGRGT DIKLDEEAVV VGGLHVIGTS RHQSRRIDRQ
LRGRCARLGD PGSAKFFLSF EDRLMRLFAS PKLNALIRHF RPPEGEAMSD PMFNKLIETA
QKRVEARNYT IRKHTLEYDD VMNRQRQTIY AFRNDVIRSE DIFGLAKEAI SHVALMIASL
IVSRDHPTGN SLPRLEEWMN YSFPLQLNIE ELKRLKSIDA IAERVADDLI EVFQNKFASM
VQEITEAAGE KVDANGVCKD VIRSVMIMHI DEQWKIHLVD MDLLRSEVGL RTVGQKDPLI
EFKHESFLLF ESLIRDIRIA IVKHLFRLEL TMTREQRPQN VVPVVATSFQ NNENFGPLEL
TVISDSDDE
