ID   A0A0G4KB94_9FLOR        Unreviewed;       869 AA.
AC   A0A0G4KB94;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ECO:0000313|EMBL:CRF40066.1};
OS   Laurencia snackeyi.
OG   Plastid {ECO:0000313|EMBL:CRF40066.1}.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Rhodomelaceae; Laurencieae; Laurencia.
OX   NCBI_TaxID=1858662 {ECO:0000313|EMBL:CRF40066.1, ECO:0000313|Proteomes:UP000307987};
RN   [1] {ECO:0000313|Proteomes:UP000307987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28061748; DOI=10.1186/s12864-016-3453-0;
RA   Ng P.K., Lin S.M., Lim P.E., Liu L.C., Chen C.M., Pai T.W.;
RT   "Complete chloroplast genome of Gracilaria firma (Gracilariaceae,
RT   Rhodophyta), with discussion on the use of chloroplast phylogenomics in the
RT   subclass Rhodymeniophycidae.";
RL   BMC Genomics 18:40-40(2017).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate +
CC         chloroplast-proteinSide 2.; EC=7.4.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034043};
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}.
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DR   EMBL; LN833431; CRF40066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4KB94; -.
DR   Proteomes; UP000307987; Chromosome plastid.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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   NCBIfam; TIGR00963; secA; 1.
DR   PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR   PANTHER; PTHR30612:SF0; SI:DKEY-187J14.7-RELATED; 1.
DR   Pfam; PF21090; P-loop_SecA; 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; 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 membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01382}; Plastid {ECO:0000313|EMBL:CRF40066.1};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
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}.
FT   DOMAIN          1..656
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          82..241
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          721..748
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         98..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         488
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   869 AA;  101139 MW;  1CA183140EB56323 CRC64;
     MFNFFPYNSI NKYKATIKEI NQQYCKIQQY SNSELKKQTE KLKLAIIQDN KNLDEILIEA
     FATVKEAIAR ATGIVLFDVQ ILGGIILHKG NIAEMKTGEG KTLVALLPAY LNTLNSTNVH
     IITVNDYLAK RDAKLAQTVF NYLNIQTGVI TSSTNYYNRK KEYKQDITYI TNNELGFDYL
     RDNMAINSND IIQSSLNYAI IDEVDSILID EARTPLIISG ETKISDNLYS KSKETSQKLE
     KKIHYQVDEK SRNVILTEKG VLVCEQILNI QNLYNINSPW LKYIVNALKA KELFLKNKDY
     IVKDNKVVIV DEFTGRIMEG RRWSDGLHQS IEAKENLKIE KENKTLASIT YQNLFLLYKK
     LCGMTGTAKT EENEFLNIYK MSVIEIPTNK QCIRKDLSDL VYQSEYSKWK AITNECIDMY
     QIGRPTLIGT TSIEKSELLA NMLDELDISY NLLNAKPENT NKEADIISEA GRKYKITIST
     NMAGRGTDII LGGNPHKVIQ ENLKKYIHSH INLSDYKVDQ VQHILNNTEV KVLNNFIEQA
     IQESQEIPAI VEDIINQKSC DKLYKISQKL SNEFTSICNK EKQEILALGG LYVIGTERHE
     SRRIDNQLRG RSGRQGDKGT SRFFLSLQDN LFRIFGGNKI KTLMKNLKID DNTPIESIVL
     SKSLNNAQKK VEAYFYDIRK QLFEYDEVIN NQRKAIYRER KAILNSYFTK DCIIEYGEYT
     IKEMIRLYEK EKRNIEILKQ IIQLLNIQQN ISIETIKTMK IKDLEQILFQ QFRISYDLKE
     TYLEQLRPGL IRQLEKYYLL QQIDKAWQDH IERMNLLKEY IGWRSYGQQE PLVEYKNEGF
     HLFINMTTYI RQTVIYLIMR SRLIIDLPN
//