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Database: UniProt
Entry: A0A2M8J274_9RHOB
LinkDB: A0A2M8J274_9RHOB
Original site: A0A2M8J274_9RHOB 
ID   A0A2M8J274_9RHOB        Unreviewed;       161 AA.
AC   A0A2M8J274;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000256|HAMAP-Rule:MF_00237};
GN   Name=tatB {ECO:0000256|HAMAP-Rule:MF_00237,
GN   ECO:0000313|EMBL:PJE36854.1};
GN   ORFNames=CVM52_09765 {ECO:0000313|EMBL:PJE36854.1};
OS   Pseudooceanicola lipolyticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE36854.1, ECO:0000313|Proteomes:UP000231553};
RN   [1] {ECO:0000313|EMBL:PJE36854.1, ECO:0000313|Proteomes:UP000231553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=157 {ECO:0000313|EMBL:PJE36854.1,
RC   ECO:0000313|Proteomes:UP000231553};
RX   PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA   Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA   Xu X.-W.;
RT   "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT   reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT   comb. nov. and emended description of the genus Pseudooceanicola.";
RL   Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
CC   -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC       transports large folded proteins containing a characteristic twin-
CC       arginine motif in their signal peptide across membranes. Together with
CC       TatC, TatB is part of a receptor directly interacting with Tat signal
CC       peptides. TatB may form an oligomeric binding site that transiently
CC       accommodates folded Tat precursor proteins before their translocation.
CC       {ECO:0000256|HAMAP-Rule:MF_00237}.
CC   -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC       complex, containing multiple copies of TatA, TatB and TatC subunits,
CC       and a separate TatA complex, containing only TatA subunits. Substrates
CC       initially bind to the TatABC complex, which probably triggers
CC       association of the separate TatA complex to form the active translocon.
CC       {ECO:0000256|HAMAP-Rule:MF_00237}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00237};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00237}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the TatB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00237}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJE36854.1}.
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DR   EMBL; PGTB01000028; PJE36854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8J274; -.
DR   OrthoDB; 7206969at2; -.
DR   Proteomes; UP000231553; Unassembled WGS sequence.
DR   GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.5.3310; -; 1.
DR   HAMAP; MF_00237; TatB; 1.
DR   InterPro; IPR003369; TatA/B/E.
DR   InterPro; IPR018448; TatB.
DR   NCBIfam; TIGR01410; tatB; 1.
DR   PANTHER; PTHR33162; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33162:SF1; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA, CHLOROPLASTIC; 1.
DR   Pfam; PF02416; TatA_B_E; 1.
DR   PRINTS; PR01506; TATBPROTEIN.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00237};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00237};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_00237}; Reference proteome {ECO:0000313|Proteomes:UP000231553};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_00237};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00237};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00237};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00237}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          81..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   161 AA;  16851 MW;  4060B819073C7E27 CRC64;
     MFDLGWTELL LIGIVALIVV GPKDLPVLFR NVGIWVGKAR GMAREFSRAM NDAADESGVK
     DVAKGLKAAT NPVSSALDGV KSATRDMTKG LDPTKYTPDS ETGKLAAERA ESAKKIQAAT
     ARAAAERKAR EAAEALAKAE EAEAALKAET PAAKREAGDS V
//
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