PSPA_MYCTU
ID PSPA_MYCTU Reviewed; 270 AA.
AC P9WHP5; L0TD78; P0C5C4; P31511;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=PspA protein {ECO:0000305};
DE AltName: Full=35 kDa protein;
GN Name=pspA {ECO:0000303|PubMed:25899163}; OrderedLocusNames=Rv2744c;
GN ORFNames=MTV002.09c;
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 ACTIVITY REGULATION, AND INTERACTION WITH PEPD.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=21445360; DOI=10.1371/journal.pone.0018175;
RA White M.J., Savaryn J.P., Bretl D.J., He H., Penoske R.M., Terhune S.S.,
RA Zahrt T.C.;
RT "The HtrA-like serine protease PepD interacts with and modulates the
RT Mycobacterium tuberculosis 35-kDa antigen outer envelope protein.";
RL PLoS ONE 6:e18175-e18175(2011).
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 FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CLGR AND RV2743C, AND
RP INDUCTION.
RX PubMed=25899163; DOI=10.1111/mmi.13037;
RA Datta P., Ravi J., Guerrini V., Chauhan R., Neiditch M.B., Shell S.S.,
RA Fortune S.M., Hancioglu B., Igoshin O.A., Gennaro M.L.;
RT "The Psp system of Mycobacterium tuberculosis integrates envelope stress-
RT sensing and envelope-preserving functions.";
RL Mol. Microbiol. 97:408-422(2015).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE,
RP AND OVEREXPRESSION.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=27002134; DOI=10.1128/jb.01001-15;
RA Armstrong R.M., Adams K.L., Zilisch J.E., Bretl D.J., Sato H.,
RA Anderson D.M., Zahrt T.C.;
RT "Rv2744c is a PspA ortholog that regulates lipid droplet homeostasis and
RT nonreplicating persistence in Mycobacterium tuberculosis.";
RL J. Bacteriol. 198:1645-1661(2016).
CC -!- FUNCTION: Involved in resistance to stress (PubMed:25899163,
CC PubMed:27002134). Facilitates intracellular growth of M.tuberculosis
CC (PubMed:25899163). Associates with and regulates lipid droplets (LDs)
CC homeostasis under conditions of stress and may regulate non-replicating
CC persistence (NRP) (PubMed:27002134). Could be involved in preservation
CC of envelope integrity and tolerance to surface stress
CC (PubMed:25899163). Has an inhibitory effect on ClgR activity
CC (PubMed:25899163). May block ClgR activity after stress and then, form
CC a multiprotein complex with Rv2743c-Rv2742c, leading to the release of
CC ClgR (PubMed:25899163). {ECO:0000269|PubMed:25899163,
CC ECO:0000269|PubMed:27002134}.
CC -!- ACTIVITY REGULATION: Levels are regulated by proteolytic cleavage by
CC PepD to help maintain cell envelope homeostasis.
CC {ECO:0000269|PubMed:21445360, ECO:0000269|PubMed:25899163}.
CC -!- SUBUNIT: Self-associates and forms homooligomeric complexes of high
CC molecular weight in vitro (PubMed:27002134). Datta et al. show that
CC PspA interacts with ClgR and Rv2743c, but Armstrong et al. fail to
CC observe interaction with either ClgR or Rv2743c in E.coli in vivo when
CC assayed using a bacterial adenylate two-hybrid assay (PubMed:25899163,
CC PubMed:27002134). Also interacts with the serine protease PepD
CC (PubMed:21445360). {ECO:0000269|PubMed:21445360,
CC ECO:0000269|PubMed:25899163, ECO:0000269|PubMed:27002134}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27002134}.
CC Note=Localizes to the surface of lipid droplets (LDs).
CC {ECO:0000269|PubMed:27002134}.
CC -!- INDUCTION: Expression is regulated by ClgR (PubMed:25899163). Induced
CC by carbonyl cyanide m-chlorophenyl hydrazone (CCCP) (PubMed:25899163).
CC Induced by the cell envelope stressor SDS (PubMed:27002134).
CC {ECO:0000269|PubMed:25899163, ECO:0000269|PubMed:27002134}.
CC -!- DISRUPTION PHENOTYPE: Loss of the gene does not alter resistance to
CC cell envelope stressors. {ECO:0000269|PubMed:27002134}.
CC -!- MISCELLANEOUS: Overexpression of PspA results in altered lipid droplet
CC morphology. {ECO:0000269|PubMed:27002134}.
CC -!- SIMILARITY: Belongs to the PspA/IM30 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45543.1; -; Genomic_DNA.
DR PIR; A60176; A60176.
DR RefSeq; WP_003414030.1; NZ_NVQJ01000020.1.
DR RefSeq; YP_177903.1; NC_000962.3.
DR AlphaFoldDB; P9WHP5; -.
DR SMR; P9WHP5; -.
DR STRING; 83332.Rv2744c; -.
DR PaxDb; P9WHP5; -.
DR DNASU; 888304; -.
DR GeneID; 45426731; -.
DR GeneID; 888304; -.
DR KEGG; mtu:Rv2744c; -.
DR TubercuList; Rv2744c; -.
DR eggNOG; COG1842; Bacteria.
DR OMA; QNAMVLQ; -.
DR PhylomeDB; P9WHP5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR InterPro; IPR007157; PspA_IM30.
DR Pfam; PF04012; PspA_IM30; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Stress response; Virulence.
FT CHAIN 1..270
FT /note="PspA protein"
FT /id="PRO_0000166290"
FT REGION 238..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 29258 MW; AB018731FF7DEC40 CRC64;
MANPFVKAWK YLMALFSSKI DEHADPKVQI QQAIEEAQRT HQALTQQAAQ VIGNQRQLEM
RLNRQLADIE KLQVNVRQAL TLADQATAAG DAAKATEYNN AAEAFAAQLV TAEQSVEDLK
TLHDQALSAA AQAKKAVERN AMVLQQKIAE RTKLLSQLEQ AKMQEQVSAS LRSMSELAAP
GNTPSLDEVR DKIERRYANA IGSAELAESS VQGRMLEVEQ AGIQMAGHSR LEQIRASMRG
EALPAGGTTA TPRPATETSG GAIAEQPYGQ
