SLPA_DEIRA
ID SLPA_DEIRA Reviewed; 1167 AA.
AC Q9RRB6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=S-layer protein SlpA {ECO:0000303|PubMed:16946272};
DE Flags: Precursor;
GN Name=slpA {ECO:0000303|PubMed:16946272};
GN OrderedLocusNames=DR_2577 {ECO:0000312|EMBL:AAF12114.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=16946272; DOI=10.1099/mic.0.28971-0;
RA Rothfuss H., Lara J.C., Schmid A.K., Lidstrom M.E.;
RT "Involvement of the S-layer proteins Hpi and SlpA in the maintenance of
RT cell envelope integrity in Deinococcus radiodurans R1.";
RL Microbiology 152:2779-2787(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=24589688; DOI=10.1016/j.bbamem.2014.02.014;
RA Farci D., Bowler M.W., Kirkpatrick J., McSweeney S., Tramontano E.,
RA Piano D.;
RT "New features of the cell wall of the radio-resistant bacterium Deinococcus
RT radiodurans.";
RL Biochim. Biophys. Acta 1838:1978-1984(2014).
RN [4]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=26074883; DOI=10.3389/fmicb.2015.00414;
RA Farci D., Bowler M.W., Esposito F., McSweeney S., Tramontano E., Piano D.;
RT "Purification and characterization of DR_2577 (SlpA) a major S-layer
RT protein from Deinococcus radiodurans.";
RL Front. Microbiol. 6:414-414(2015).
RN [5]
RP FUNCTION, DEINOXANTHIN-BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=26909071; DOI=10.3389/fmicb.2016.00155;
RA Farci D., Slavov C., Tramontano E., Piano D.;
RT "The S-layer protein DR_2577 binds deinoxanthin and under desiccation
RT conditions protects against UV-radiation in Deinococcus radiodurans.";
RL Front. Microbiol. 7:155-155(2016).
CC -!- FUNCTION: Major constituent of the S-layer. Plays an important role in
CC the structural organization and integrity of the S-layer
CC (PubMed:16946272, PubMed:26074883). Binds the carotenoid deinoxanthin,
CC a strong protective antioxidant specific of this bacterium, and could
CC be part of the first lane of defense against UV radiation, especially
CC under desiccation (PubMed:26909071). {ECO:0000269|PubMed:16946272,
CC ECO:0000269|PubMed:26074883, ECO:0000269|PubMed:26909071}.
CC -!- SUBUNIT: Homohexamer; trimer of disulfide-linked dimers.
CC {ECO:0000269|PubMed:26074883}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:24589688, ECO:0000269|PubMed:26074883}.
CC -!- DISRUPTION PHENOTYPE: Deletion causes substantial alterations in cell
CC envelope structure, and a significant defect in resistance to solvent
CC and shear stresses. Mutants shed exterior layers of the cellular
CC envelope (PubMed:16946272). Deletion mutants show a significant
CC decrease of the UV resistance, especially under desiccation conditions
CC (PubMed:26909071). {ECO:0000269|PubMed:16946272,
CC ECO:0000269|PubMed:26909071}.
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DR EMBL; AE000513; AAF12114.1; -; Genomic_DNA.
DR PIR; B75258; B75258.
DR RefSeq; NP_296297.1; NC_001263.1.
DR RefSeq; WP_010889202.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RRB6; -.
DR STRING; 243230.DR_2577; -.
DR PRIDE; Q9RRB6; -.
DR EnsemblBacteria; AAF12114; AAF12114; DR_2577.
DR KEGG; dra:DR_2577; -.
DR PATRIC; fig|243230.17.peg.2823; -.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_310736_0_0_0; -.
DR OMA; GAYYRDV; -.
DR OrthoDB; 42763at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR InterPro; IPR001119; SLH_dom.
DR Pfam; PF00395; SLH; 1.
DR PROSITE; PS51272; SLH; 1.
PE 1: Evidence at protein level;
KW Cell wall; Disulfide bond; Reference proteome; S-layer; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1167
FT /note="S-layer protein SlpA"
FT /id="PRO_5004333117"
FT DOMAIN 29..92
FT /note="SLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DISULFID 929
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:26074883"
SQ SEQUENCE 1167 AA; 123730 MW; 7FFCA45F15115462 CRC64;
MKKSLIALTT ALSFGLAAAQ TAAPVSAPQV PALTDVPAGH WAKDAIDRLV SRGVILGYPD
GTFRGTQNLT RYEAAIIIAR LLDQMRDGET PAGMTAEDMT ALQNAIQELA ADLAALGVRV
SDLEANAVSK DDFARLEARI EEVAAAGGEQ GATEALQGQI DDLTARVDEY DALRADVDDN
ASSIAALNDL TVLLNQDILD LQDRVSAVEA AQADFVQRSD FDALGGRVTT VETRVETVNN
SLTGRIAALE RNAFSVKPSL TIGYSVSRTS RNFDVDRLFP LNADGTVANN AFTSGGIDTD
TGAQRRDFGD FGNASDPVVA GAAGLYGFAD GVSYTVYFTD GSTATFDGLN PADYKVPTGK
VIDTTKGRNG FGFNNLARYK EGSTDIGISL GFDTSGQFSQ VTSGTGGSLF STAGRLQVNQ
IDLNFGLVTG LPSDAYVDTN GNGKKDDGEA TGRGTYLGSG GTAAILRDPA GNVYRPVFFR
FKNATTQFSV GNNPVIVTLG QQQKFYFSDY VFDNNYDGRG DGFTVTVDGS NVPVIGAWKP
QIKGVYGSRS GLDGTAEAGY GVYYRGVRAQ ITPVGTLTAG IHYAQEGRDM FGAAQNTTST
PSDVTTYGAD LHGKAFGVEL HSEYATSRVR PNTANAAVQT SNAFYARVAT RKDNLAFDLN
TPAAKFGNDT FGVSLYDLNY RKIDAGYNNV AGISEYGYGS YSRTSAQNIA YNPDTGVTAP
FANLDRQAYT DANNDGTSDR NADGTVVATN TKIGQMGFGV KAAANLGPVA IGGYYDTSTG
ANGDNANRMT EAGGSAKVAY SIFSLRGTYN TLDSNRPQIY RDAAGTQIIG DAKVRRYAVQ
ADVTPGLGLF VGAYYRDVNV NGVRSTTDRG LLGRGYLASS FEPGVGNNAY RTGLRCADNN
FGTGTRDIDG VGGVLNPAVN LDQSRTATCF TSYGVEAGHA GDNANALVKD LFFRVGYSRV
YVPTTATATT GDFSGSVTYG DARYDRKVGV ANVRLAGSFS TTNTQLDSRP AGTRGAVGLI
VRTDPLENVP FRPQFNGQVG YYTADNRVAA GNYNANATKY GAGVVLNDFL LPQTKIGVRY
DGYMAQNRQY TPFDGDGTQG YFSDANNNRR TNLNGVYVEG AYQDLIFSYG TYTLSQKDLN
GVEYGSGINN GQPARGQTFK ISYKVNF
