ID   CBIB_SALPB              Reviewed;         319 AA.
AC   A9MT86;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cobalamin biosynthesis protein CbiB {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cbiB {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=SPAB_01071;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. However, the true cosubstrate
CC       could be (R)-1-amino-2-propanol O-2-phosphate, leading to cobinamide
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00024};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
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DR   EMBL; CP000886; ABX66492.1; -; Genomic_DNA.
DR   RefSeq; WP_000153660.1; NC_010102.1.
DR   AlphaFoldDB; A9MT86; -.
DR   KEGG; spq:SPAB_01071; -.
DR   PATRIC; fig|1016998.12.peg.1012; -.
DR   HOGENOM; CLU_054212_0_0_6; -.
DR   OMA; WGYRNER; -.
DR   BioCyc; SENT1016998:SPAB_RS04475-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008556; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00024; CobD_CbiB; 1.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
DR   TIGRFAMs; TIGR00380; cobD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalamin biosynthesis; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..319
FT                   /note="Cobalamin biosynthesis protein CbiB"
FT                   /id="PRO_1000074384"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   319 AA;  35410 MW;  E87DBD7C54B9EDD2 CRC64;
     MTILAWCIAW VLDFIIGDPQ HWPHPVRWIG RLITFVQRIV RRYCPGDKAL RIGGGVMWVV
     VVGATWGVAW GVLALAQRIH PWFGWSVEVW MIFTTLAGRS LARAAQEVER PLRENDLAES
     RIKLSWIVGR DTSQLQPAQI NRGVVETVAE NTVDGIIAPL FFLFLGGAPL AMAYKAVNTL
     DSMVGYKHEK YRAIGMVSAR MDDVANYLPA RLSWLLLGIA AGLCRLSGWR ALRIGWRDRY
     NHSSPNCAWS EACVAGALGI QLGGPNNYFG ERVDKPWIGD AQRDISVDDI SRTIRLMWVA
     STLALALFIA ARCGLSGVA