FHAA_MYCTU
ID FHAA_MYCTU Reviewed; 527 AA.
AC P71590; F2GPM4; L0T599;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=FHA domain-containing protein FhaA;
GN Name=fhaA; Synonyms=TB39.8; OrderedLocusNames=Rv0020c;
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 PHOSPHORYLATION BY PKNB, AND MUTAGENESIS OF ARG-459 AND SER-473.
RX PubMed=15987910; DOI=10.1110/ps.051413405;
RA Grundner C., Gay L.M., Alber T.;
RT "Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and
RT PknF phosphorylate multiple FHA domains.";
RL Protein Sci. 14:1918-1921(2005).
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 431-527.
RX PubMed=21134638; DOI=10.1016/j.str.2010.09.014;
RA Pennell S., Westcott S., Ortiz-Lombardia M., Patel D., Li J., Nott T.J.,
RA Mohammed D., Buxton R.S., Yaffe M.B., Verma C., Smerdon S.J.;
RT "Structural and functional analysis of phosphothreonine-dependent FHA
RT domain interactions.";
RL Structure 18:1587-1595(2010).
RN [5]
RP STRUCTURE BY NMR OF 1-132, INTERACTION WITH PKNB, DOMAIN, PHOSPHORYLATION
RP AT THR-116, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP THR-116.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22000520; DOI=10.1016/j.str.2011.07.011;
RA Roumestand C., Leiba J., Galophe N., Margeat E., Padilla A., Bessin Y.,
RA Barthe P., Molle V., Cohen-Gonsaud M.;
RT "Structural insight into the Mycobacterium tuberculosis Rv0020c protein and
RT its interaction with the PknB kinase.";
RL Structure 19:1525-1534(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 390-525, FUNCTION, INTERACTION
RP WITH MVIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-459; GLN-461 AND
RP ARG-474.
RX PubMed=22275220; DOI=10.1126/scisignal.2002525;
RA Gee C.L., Papavinasasundaram K.G., Blair S.R., Baer C.E., Falick A.M.,
RA King D.S., Griffin J.E., Venghatakrishnan H., Zukauskas A., Wei J.R.,
RA Dhiman R.K., Crick D.C., Rubin E.J., Sassetti C.M., Alber T.;
RT "A phosphorylated pseudokinase complex controls cell wall synthesis in
RT mycobacteria.";
RL Sci. Signal. 5:RA7-RA7(2012).
CC -!- FUNCTION: Regulates cell growth and peptidoglycan synthesis by binding
CC to MviN. May inhibit the late stages of peptidoglycan synthesis.
CC {ECO:0000269|PubMed:22275220}.
CC -!- SUBUNIT: Interacts with (phosphorylated) MviN and (phosphorylated) PknB
CC via the FHA domain. Binds to the PknB juxtamembrane domain with an
CC affinity that is modulated by the degree and the pattern of
CC phosphorylation of this juxtamembrane domain.
CC {ECO:0000269|PubMed:22000520, ECO:0000269|PubMed:22275220}.
CC -!- INTERACTION:
CC P71590; P9WI81: pknB; NbExp=4; IntAct=EBI-15896562, EBI-2946037;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22275220}.
CC Note=Localizes at the cell poles and at the septum.
CC -!- DOMAIN: The structure of the N-terminal domain remains unchanged upon
CC phosphorylation. {ECO:0000269|PubMed:22000520}.
CC -!- PTM: Phosphorylated by PknB. {ECO:0000269|PubMed:15987910,
CC ECO:0000269|PubMed:22000520}.
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DR EMBL; AL123456; CCP42742.1; -; Genomic_DNA.
DR PIR; B70700; B70700.
DR RefSeq; NP_214534.1; NC_000962.3.
DR RefSeq; WP_003912368.1; NZ_NVQJ01000005.1.
DR PDB; 2LC0; NMR; -; A=1-132.
DR PDB; 2LC1; NMR; -; A=430-527.
DR PDB; 3OUN; X-ray; 2.70 A; A=390-525.
DR PDB; 3PO8; X-ray; 1.50 A; A=431-527.
DR PDB; 3POA; X-ray; 2.01 A; A=431-527.
DR PDBsum; 2LC0; -.
DR PDBsum; 2LC1; -.
DR PDBsum; 3OUN; -.
DR PDBsum; 3PO8; -.
DR PDBsum; 3POA; -.
DR AlphaFoldDB; P71590; -.
DR BMRB; P71590; -.
DR SMR; P71590; -.
DR DIP; DIP-59047N; -.
DR IntAct; P71590; 1.
DR STRING; 83332.Rv0020c; -.
DR iPTMnet; P71590; -.
DR PaxDb; P71590; -.
DR GeneID; 887067; -.
DR KEGG; mtu:Rv0020c; -.
DR TubercuList; Rv0020c; -.
DR eggNOG; COG1716; Bacteria.
DR InParanoid; P71590; -.
DR OMA; DQRGGYP; -.
DR EvolutionaryTrace; P71590; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR CDD; cd00060; FHA; 1.
DR DisProt; DP01671; -.
DR Gene3D; 3.30.2320.60; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022128; FhaA_N.
DR InterPro; IPR042287; FhaA_N_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF12401; DUF3662; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..527
FT /note="FHA domain-containing protein FhaA"
FT /id="PRO_0000419664"
FT DOMAIN 455..504
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 119..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22000520"
FT MUTAGEN 116
FT /note="T->A: Lack of phosphorylation."
FT /evidence="ECO:0000269|PubMed:22000520"
FT MUTAGEN 459
FT /note="R->A: Abolishes phosphorylation by PknB. Strong
FT decrease in affinity for MviN."
FT /evidence="ECO:0000269|PubMed:15987910,
FT ECO:0000269|PubMed:22275220"
FT MUTAGEN 461
FT /note="Q->A: Does not affect affinity for MviN."
FT /evidence="ECO:0000269|PubMed:22275220"
FT MUTAGEN 473
FT /note="S->A: Abolishes phosphorylation by PknB."
FT /evidence="ECO:0000269|PubMed:15987910"
FT MUTAGEN 474
FT /note="R->A: Decrease in affinity for MviN."
FT /evidence="ECO:0000269|PubMed:22275220"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2LC0"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:2LC0"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2LC0"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:2LC0"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:2LC0"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2LC0"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2LC0"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2LC0"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 452..460
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2LC1"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:3POA"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:3PO8"
FT STRAND 520..527
FT /evidence="ECO:0007829|PDB:3PO8"
SQ SEQUENCE 527 AA; 56880 MW; 2642F9CF23FE7906 CRC64;
MGSQKRLVQR VERKLEQTVG DAFARIFGGS IVPQEVEALL RREAADGIQS LQGNRLLAPN
EYIITLGVHD FEKLGADPEL KSTGFARDLA DYIQEQGWQT YGDVVVRFEQ SSNLHTGQFR
ARGTVNPDVE THPPVIDCAR PQSNHAFGAE PGVAPMSDNS SYRGGQGQGR PDEYYDDRYA
RPQEDPRGGP DPQGGSDPRG GYPPETGGYP PQPGYPRPRH PDQGDYPEQI GYPDQGGYPE
QRGYPEQRGY PDQRGYQDQG RGYPDQGQGG YPPPYEQRPP VSPGPAAGYG APGYDQGYRQ
SGGYGPSPGG GQPGYGGYGE YGRGPARHEE GSYVPSGPPG PPEQRPAYPD QGGYDQGYQQ
GATTYGRQDY GGGADYTRYT ESPRVPGYAP QGGGYAEPAG RDYDYGQSGA PDYGQPAPGG
YSGYGQGGYG SAGTSVTLQL DDGSGRTYQL REGSNIIGRG QDAQFRLPDT GVSRRHLEIR
WDGQVALLAD LNSTNGTTVN NAPVQEWQLA DGDVIRLGHS EIIVRMH
