ID A9FG49_SORC5 Unreviewed; 410 AA.
AC A9FG49;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Penicillin-insensitive murein endopeptidase {ECO:0000313|EMBL:CAN98087.1};
GN OrderedLocusNames=sce7917 {ECO:0000313|EMBL:CAN98087.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN98087.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN98087.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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DR EMBL; AM746676; CAN98087.1; -; Genomic_DNA.
DR RefSeq; WP_012240526.1; NC_010162.1.
DR AlphaFoldDB; A9FG49; -.
DR STRING; 448385.sce7917; -.
DR KEGG; scl:sce7917; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3770; Bacteria.
DR HOGENOM; CLU_670653_0_0_7; -.
DR OrthoDB; 5502029at2; -.
DR BioCyc; SCEL448385:SCE_RS40530-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR005073; Peptidase_M74.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03411; Peptidase_M74; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002738462"
FT DOMAIN 322..365
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 35..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 44155 MW; B2388A74314E7AA5 CRC64;
MGRSSLVSVL CALLLAGCAG RAPEAARSKD SLLRVASGVS SEQRGASPAP GTAAEEAALA
DDHDAEVDDD DGEVDDGLEP PADPGTGARA HSPLSAMTEA QIEELFSKDP AALGPMSLGA
TNAGALFNGV RMPEGDRWEL VDPAHAWGTR ETIDALDRAI AEVHRQFPGS PKLYIGHISA
REGGRLSPHK SHQAGRDVDI SYFLDARHRW YQRATAANLD RERTWAFVRA LVTETDVELI
LIDSSVQRLL KEHALKIGED KDWLDEVFQL GSRKPRPLIR HARGHANHIH VRFYSPVAQE
SAARAYPLLV KRGAIKPTSQ YVRHTAKKGQ TLGSLARQYG TTVEAIKRAN GLRSTAIQAK
RVYNIPRPSS GPAAPPKQIV VPPRRLPPPK AADAPPPPAR HGEPGPALDG
//
