FHAB_MYCTU
ID FHAB_MYCTU Reviewed; 155 AA.
AC P9WJB5; F2GPM3; L0T5G4; P71589; Q7DAK4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=FHA domain-containing protein FhaB;
DE AltName: Full=FtsZ-interacting protein A;
GN Name=fhaB; Synonyms=fipA; OrderedLocusNames=Rv0019c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INTERACTION WITH PKNB AND PAPA5, PHOSPHORYLATION AT THR-36,
RP DEPHOSPHORYLATION, AND MUTAGENESIS OF THR-36; THR-50; ARG-87 AND SER-101.
RX PubMed=19826007; DOI=10.1074/jbc.m109.058834;
RA Gupta M., Sajid A., Arora G., Tandon V., Singh Y.;
RT "Forkhead-associated domain-containing protein Rv0019c and polyketide-
RT associated protein PapA5, from substrates of serine/threonine protein
RT kinase PknB to interacting proteins of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:34723-34734(2009).
RN [3]
RP RETRACTED PAPER.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066037; DOI=10.1371/journal.pone.0008590;
RA Sureka K., Hossain T., Mukherjee P., Chatterjee P., Datta P., Kundu M.,
RA Basu J.;
RT "Novel role of phosphorylation-dependent interaction between FtsZ and FipA
RT in mycobacterial cell division.";
RL PLoS ONE 5:E8590-E8590(2010).
RN [4]
RP RETRACTION NOTICE OF PUBMED:20066037.
RX PubMed=35202441; DOI=10.1371/journal.pone.0264672;
RG PLOS ONE Editors;
RL PLoS ONE 17:e0264672-e0264672(2022).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- SUBUNIT: Interacts with (phosphorylated) PknB via the FHA domain.
CC Interacts with PapA5 via a phosphoindependent interaction involving N-
CC terminal residues preceding the FHA domain.
CC {ECO:0000269|PubMed:19826007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: Phosphorylated by PknB (PubMed:19826007). Dephosphorylated by PstP
CC (PubMed:19826007). {ECO:0000269|PubMed:19826007}.
CC -!- CAUTION: The article by Sureka et al was retracted by the editors after
CC publication. Concerns were raised regarding the results presented in
CC multiple figure panels. The raw data or replacement panels that were
CC available did not satisfactorily address all the issues, thus
CC questioning the integrity of the data. {ECO:0000305|PubMed:35202441}.
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DR EMBL; AL123456; CCP42741.1; -; Genomic_DNA.
DR PIR; A70700; A70700.
DR RefSeq; NP_214533.1; NC_000962.3.
DR RefSeq; WP_003400373.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WJB5; -.
DR SMR; P9WJB5; -.
DR STRING; 83332.Rv0019c; -.
DR iPTMnet; P9WJB5; -.
DR PaxDb; P9WJB5; -.
DR GeneID; 45423978; -.
DR GeneID; 887079; -.
DR KEGG; mtu:Rv0019c; -.
DR TubercuList; Rv0019c; -.
DR eggNOG; COG1716; Bacteria.
DR OMA; MQYLLVT; -.
DR PhylomeDB; P9WJB5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0051301; P:cell division; IMP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032030; YscD_cytoplasmic_dom.
DR Pfam; PF16697; Yop-YscD_cpl; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..155
FT /note="FHA domain-containing protein FhaB"
FT /id="PRO_0000419671"
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 83..132
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT MOD_RES 36
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000269|PubMed:19826007"
FT MUTAGEN 36
FT /note="T->A: Lack of phosphorylation."
FT /evidence="ECO:0000269|PubMed:19826007"
FT MUTAGEN 50
FT /note="T->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:19826007"
FT MUTAGEN 87
FT /note="R->A: Impairs interaction with PknB and PapA5."
FT /evidence="ECO:0000269|PubMed:19826007"
FT MUTAGEN 101
FT /note="S->A: Impairs interaction with PknB. Does not affect
FT interaction with PapA5."
FT /evidence="ECO:0000269|PubMed:19826007"
SQ SEQUENCE 155 AA; 17152 MW; 5FEEAF0205FA54B9 CRC64;
MQGLVLQLTR AGFLMLLWVF IWSVLRILKT DIYAPTGAVM MRRGLALRGT LLGARQRRHA
ARYLVVTEGA LTGARITLSE QPVLIGRADD STLVLTDDYA STRHARLSMR GSEWYVEDLG
STNGTYLDRA KVTTAVRVPI GTPVRIGKTA IELRP
