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Database: UniProt
Entry: A0A172ZLG8_9BACL
LinkDB: A0A172ZLG8_9BACL
Original site: A0A172ZLG8_9BACL 
ID   A0A172ZLG8_9BACL        Unreviewed;       817 AA.
AC   A0A172ZLG8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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:ANF98476.1};
GN   ORFNames=AR543_22440 {ECO:0000313|EMBL:ANF98476.1};
OS   Paenibacillus bovis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF98476.1, ECO:0000313|Proteomes:UP000078148};
RN   [1] {ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA   Wu Z., Gao C., Liu Z., Zheng H.;
RT   "Genome of Paenibacillus bovis sp. nov.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANF98476.1, ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|EMBL:ANF98476.1,
RC   ECO:0000313|Proteomes:UP000078148};
RX   PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA   Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT   "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT   milk.";
RL   Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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   -!- 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; CP013023; ANF98476.1; -; Genomic_DNA.
DR   RefSeq; WP_060536512.1; NZ_CP013023.1.
DR   AlphaFoldDB; A0A172ZLG8; -.
DR   STRING; 1616788.AR543_22440; -.
DR   KEGG; pbv:AR543_22440; -.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000078148; 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: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; 3.
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; 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   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; 2.
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; PS51194; HELICASE_CTER; 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};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01382};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000078148};
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          2..571
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          88..246
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          419..587
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          786..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         104..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   817 AA;  93614 MW;  5C4ADDADEF46F602 CRC64;
     MLGIVKKIFG DTNERDVKRI MKTVDIINNM EPEFEALSHD ELQGKTAEFR ERLEKGETLE
     QLLPEAFATV REAAKRQLGM RHFDVQMIGG IALHEGKISE MRTGEGKTLV GTLPVYLNAL
     EGKGAHVVTV NDYLAKRDSL QMGRIYNYLG MEVGVNLSGM KHEEKQAAYA CDITYGTNNE
     FGFDYLRDNM VLYKEQMVQR PLHFCIIDEV DSILIDEART PLIISGQAQK STELYFAADR
     FVKSLKAEDD YTVDIKVKSV ALTETGVEKA ENFFGLENLY DNGNVTINHH VVQALKANAI
     MHRDVDYVVA DGEVLIVDEF TGRLMAGRRY SDGLHQAIEA KENLDVQNES MTLATITFQN
     YFRMYKKLAG MTGTAKTEEE EFKKIYGLEV LQVPTNRINQ RKDAPDVVYK SVQSKFRAVV
     DEIVVRHEKN QPVLVGTVSI ENSELLSEML KRKGIKHQVL NAKYHAEEAE IISRAGQPGT
     VTIATNMAGR GTDIILGEGV AEVGGLHIIG TERHESRRID NQLRGRAGRQ GDPGSTQFYL
     SLGDELMKRF GADNVMNMME KLGFEEDQPI ESRMITRAVE SAQRRVEGSN FDMRKIVLQY
     DDVMNKQREI IYKQRREVLE SDNIREVVLQ MIKPCIERVV EVHCNDDIPE NWELQEVADY
     VNNNFLLENA ISEAELHEQE KEEMVNYLFE RVELRYLQRE KEIGEETIRE FEKVVVLRAV
     DRKWMDHIDA MEQLRQGIHL RAYGGTDPLR EYQFEGFEMF NQMVADIQEE VAGYVMRAQI
     QTQQERQAVV DTSQVSTNSS ESAEKRPSRE ERRRRRK
//
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