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Database: UniProt
Entry: A0A1H3K0M4_9RHOB
LinkDB: A0A1H3K0M4_9RHOB
Original site: A0A1H3K0M4_9RHOB 
ID   A0A1H3K0M4_9RHOB        Unreviewed;       602 AA.
AC   A0A1H3K0M4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Sporulation related domain-containing protein {ECO:0000313|EMBL:SDY45742.1};
GN   ORFNames=SAMN05444340_10898 {ECO:0000313|EMBL:SDY45742.1};
OS   Citreimonas salinaria.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Citreimonas.
OX   NCBI_TaxID=321339 {ECO:0000313|EMBL:SDY45742.1, ECO:0000313|Proteomes:UP000199286};
RN   [1] {ECO:0000313|EMBL:SDY45742.1, ECO:0000313|Proteomes:UP000199286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26880 {ECO:0000313|EMBL:SDY45742.1,
RC   ECO:0000313|Proteomes:UP000199286};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNPF01000008; SDY45742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3K0M4; -.
DR   STRING; 321339.SAMN05444340_10898; -.
DR   OrthoDB; 6810892at2; -.
DR   Proteomes; UP000199286; Unassembled WGS sequence.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199286};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..602
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011490515"
FT   DOMAIN          28..90
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|Pfam:PF05036"
FT   DOMAIN          178..231
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   REGION          120..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  64062 MW;  58EA1301C1AE0911 CRC64;
     MLKKLMAALA LAGALTVAAQ TEARAQQQAY FIQVEAESSL TGARETARSY GDVFDNAASF
     ALGGGWYGIA LGPYTQDEAE RVLANLQGRG QIPPDSYVQD AGRYDEQVWP PGADRASTMA
     RLDASGSSSS EDALAQALGA AQDGAQDAQD TQQQAARDTA PEPETPEQAR ASERELTRAE
     REQLQIALQW AGHYGGRIDA AFGPNTRNAM RSWQQANGYE TTGILTTAQR AQVLEQYNSV
     FDGLGFARHV DDRAGIAMEI PLGVVAFDGY EPPFAKFEPT TDLGARVLLI SRPGDRQTLG
     GLYEIMQTLE IVPLEGERNR SNDGFVLKGA NDAIVSHTEV GLADGALKGF TLIWPAGDEA
     RRTRVLARMQ ESFERRPGVL EAPAALADDP AVDLVAGLRV RQPVRSTSGF FVDRAGRVLT
     SAAGVQGCAR VTLDSEHEAQ VVAQDAELGL AVLRPEDALA PRRVAQFRAD PPRLRSEVAV
     AGYSFGGVLG APTLTFGTLE EMQGLRGEDA LKRLTLASQP GDAGGPVLDD AGAVLGMLLP
     RDDQDNRRLP QDVSFAAKTD EIMAFLRGAG IDARAGGAGG ALDPVDLTRV GAEMTVLVSC
     WD
//
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