ID   TAMB_CITRI              Reviewed;        1259 AA.
AC   D2TN57;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Translocation and assembly module subunit TamB;
DE   AltName: Full=Autotransporter assembly factor TamB;
GN   Name=tamB; OrderedLocusNames=ROD_32821;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/jb.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
RN   [2]
RP   FUNCTION IN PROTEIN TRANSLOCATION, SUBCELLULAR LOCATION, SUBUNIT,
RP   INTERACTION WITH TAMA, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ICC169;
RX   PubMed=22466966; DOI=10.1038/nsmb.2261;
RA   Selkrig J., Mosbahi K., Webb C.T., Belousoff M.J., Perry A.J., Wells T.J.,
RA   Morris F., Leyton D.L., Totsika M., Phan M.D., Celik N., Kelly M.,
RA   Oates C., Hartland E.L., Robins-Browne R.M., Ramarathinam S.H.,
RA   Purcell A.W., Schembri M.A., Strugnell R.A., Henderson I.R., Walker D.,
RA   Lithgow T.;
RT   "Discovery of an archetypal protein transport system in bacterial outer
RT   membranes.";
RL   Nat. Struct. Mol. Biol. 19:506-510(2012).
CC   -!- FUNCTION: Part of the translocation and assembly module (TAM)
CC       autotransporter assembly complex, which functions in translocation of
CC       autotransporters across the outer membrane (PubMed:22466966). Substrate
CC       binding to TamA moves its POTRA domains about 30 Angstroms into the
CC       periplasm, which would deform either the outer membrane or TamB and may
CC       provide force to reset TAM (By similarity).
CC       {ECO:0000250|UniProtKB:P39321, ECO:0000269|PubMed:22466966}.
CC   -!- SUBUNIT: Interacts with TamA. {ECO:0000269|PubMed:22466966}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22466966}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:22466966}.
CC   -!- DOMAIN: The periplasmic domain is elongated (up to 160 Angstroms long)
CC       and forms contacts to the N-terminal POTRA domains of TamA.
CC       {ECO:0000250|UniProtKB:P39321}.
CC   -!- DISRUPTION PHENOTYPE: 50-fold reduction in ability to colonize mice in
CC       competitive assays with wild-type. {ECO:0000269|PubMed:22466966}.
CC   -!- SIMILARITY: Belongs to the TamB family. {ECO:0000305}.
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DR   EMBL; FN543502; CBG90001.1; -; Genomic_DNA.
DR   RefSeq; WP_012907369.1; NC_013716.1.
DR   AlphaFoldDB; D2TN57; -.
DR   SMR; D2TN57; -.
DR   DIP; DIP-59928N; -.
DR   IntAct; D2TN57; 1.
DR   STRING; 637910.ROD_32821; -.
DR   KEGG; cro:ROD_32821; -.
DR   eggNOG; COG2911; Bacteria.
DR   HOGENOM; CLU_002338_0_1_6; -.
DR   OMA; NTAKQWP; -.
DR   OrthoDB; 754526at2; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   InterPro; IPR007452; TamB.
DR   Pfam; PF04357; TamB; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..1259
FT                   /note="Translocation and assembly module subunit TamB"
FT                   /id="PRO_5000565834"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        28..1259
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1259 AA;  136339 MW;  DEF5709DA52F70AF CRC64;
     MSLWKKISLG VLIFILLLLA TVGFLVGTTT GLHLVFSAAN RWVPGLEIGQ VTGGWRDLSL
     KNIRYDQPGV AVNAGEVHLA VGLECLWKSS LCVNDLSLKD INVVIDSKKM PPGEQVEEEE
     ESGPLNLSTP YPVTLSRVAL ENINVKIDDT TVSVMDFTSG LNWQEKNLTL KPTALQGLLI
     ALPKVAEVAQ EEVVEPKIQN PQPDEKPLGE TLQDLFSKPV LPEMTDVHLP LNLNIEEFKG
     EQLRLTGDTD LTVFSLLLKV SSIDGNMKLD ALDIDSSQGA VNATGTAQLA NNWPVDITLN
     STLNVEPLKG EKIKLKVGGA LREQLEVGVN LSGPLDVNLR AQARLAEAGL PLNLEVVSEQ
     ISWPFTGDRQ FQADNTRLKL TGKMTDYTLS MRTAVKGQDV PPATITLDAK GNEQQINLDK
     LTVAALEGKT ELKALVDWRQ AISWRGELTL DGINTAKEVP DWPSKLNGLI KTRGSLYGGS
     WQMEVPELKL TGNVKQNKVN VNGSLKGNSY MQWTIPGLHL VLGPNSADVK GELGVKDLNL
     DATIDAPGLD NALPGLGGTA KGLVKVRGTV DAPQLLADIT ARGLRWQELS IAQVRVDGDI
     KSTDQIAGKL DVRVERISQP DVNINLVTLH AKGSEKQHEL QLRIQGEPVS GQLDLAGSFD
     REEMRWKGTL SNTRFRTPVG PWSQTRAIAL DYRGQEQKIS IGPHCWTNPN AELCVPQTID
     AGAEGRAVVN LNRFDLAMLK PFMPETTQAS GVFSGKADVA WDTTKEGLPQ GNVTLSGRSV
     KVTQTVNDAP LPLAFDTLNV SADLHDNRAE LGWQIRLSNN GQLDGQVQVT DPQGRRNLGG
     NVSIRNLNLA MVNPIFARGE KAAGLLNANL RLGGDVQSPQ MFGQLQLNGV DIDGNFMPFD
     MQPSQLAMNF NGTRSTLTGV VRTQQGEINL SGDADWSQIE NWRARIAAKG SRVRITVPPM
     VRLDVSPDVV FEATPSLFTL DGRVDVPWAR IVVHELPESA VGVSSDEVML NNQLQPEEPQ
     TAAIPINSNL IVHVGNNVRM DAFGLRARLT GDLKVAQDKQ GLGLNGQINI PEGRFHAYGQ
     DLLVRKGELL FSGPPDQPIL NIEAIRNPEA TEDDVIAGVR VTGSADEPKA EIFSDPAMSQ
     QEALSYLLRG QGLDSNQSDS AAMTSMLIGL GVAQSGQVVG KIGETFGVSN LALDTQGVGD
     SSQVVVSGYV LPGLQVKYGV GIFDSLATLT LRYRLMPKLY LEAVSGVDQA LDLLYQFEF