ID   SECB_METPP              Reviewed;         163 AA.
AC   A2SDN9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=Mpe_A0716;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- FUNCTION: One of the proteins required for the normal export of
CC       preproteins out of the cell cytoplasm. It is a molecular chaperone that
CC       binds to a subset of precursor proteins, maintaining them in a
CC       translocation-competent state. It also specifically binds to its
CC       receptor SecA. {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SUBUNIT: Homotetramer, a dimer of dimers. One homotetramer interacts
CC       with 1 SecA dimer. {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SIMILARITY: Belongs to the SecB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00821}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM93678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000555; ABM93678.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_036230692.1; NC_008825.1.
DR   AlphaFoldDB; A2SDN9; -.
DR   SMR; A2SDN9; -.
DR   STRING; 420662.Mpe_A0716; -.
DR   PRIDE; A2SDN9; -.
DR   EnsemblBacteria; ABM93678; ABM93678; Mpe_A0716.
DR   KEGG; mpt:Mpe_A0716; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_1_0_4; -.
DR   OrthoDB; 1624074at2; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.420.10; -; 1.
DR   HAMAP; MF_00821; SecB; 1.
DR   InterPro; IPR003708; SecB.
DR   InterPro; IPR035958; SecB-like_sf.
DR   PANTHER; PTHR36918; PTHR36918; 1.
DR   Pfam; PF02556; SecB; 1.
DR   PRINTS; PR01594; SECBCHAPRONE.
DR   SUPFAM; SSF54611; SSF54611; 1.
DR   TIGRFAMs; TIGR00809; secB; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Protein transport; Reference proteome; Translocation;
KW   Transport.
FT   CHAIN           1..163
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_0000318246"
SQ   SEQUENCE   163 AA;  17457 MW;  8AB20313F1FD41AC CRC64;
     MAEQDSNPVF QIQRVYLKDV SLEQPNSPQI LLEQSQPQVD ISLAVNAETV ADGIYEVSVT
     ATVTTKVADK TLFLCEAKQA GIFEIRNLPD GQTQPVLGIA CPGIVYPYLR ATVADIITRA
     GFPPVHLAEV NFQAMYEAQQ QAAAQQQGAV SNGNGGSPII TNA