FLGJ_SALTY
ID FLGJ_SALTY Reviewed; 316 AA.
AC P15931;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Peptidoglycan hydrolase FlgJ;
DE EC=3.2.1.-;
DE AltName: Full=Muramidase FlgJ;
GN Name=flgJ; Synonyms=fla FX, flaZ; OrderedLocusNames=STM1182;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544561; DOI=10.1128/jb.171.7.3890-3900.1989;
RA Jones C.J., Homma M., Macnab R.M.;
RT "L-, P-, and M-ring proteins of the flagellar basal body of Salmonella
RT typhimurium: gene sequences and deduced protein sequences.";
RL J. Bacteriol. 171:3890-3900(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-316.
RX PubMed=2193164; DOI=10.1016/s0022-2836(05)80266-9;
RA Homma M., Derosier D.J., Macnab R.M.;
RT "Flagellar hook and hook-associated proteins of Salmonella typhimurium and
RT their relationship to other axial components of the flagellum.";
RL J. Mol. Biol. 213:819-832(1990).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLU-223 AND ASP-248.
RX PubMed=10049388; DOI=10.1128/jb.181.5.1555-1561.1999;
RA Nambu T., Minamino T., Macnab R.M., Kutsukake K.;
RT "Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for
RT flagellar rod formation in Salmonella typhimurium.";
RL J. Bacteriol. 181:1555-1561(1999).
CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC peptidoglycan layer to assemble the rod structure in the periplasmic
CC space. {ECO:0000269|PubMed:10049388}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: Exported via the flagellum-specific export pathway.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 73 family. {ECO:0000305}.
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DR EMBL; M24466; AAA27070.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20112.1; -; Genomic_DNA.
DR EMBL; X51738; CAA36024.1; -; Genomic_DNA.
DR PIR; D32887; C30930.
DR RefSeq; NP_460153.1; NC_003197.2.
DR RefSeq; WP_000578692.1; NC_003197.2.
DR PDB; 5DN4; X-ray; 1.80 A; A=151-316.
DR PDB; 5DN5; X-ray; 2.15 A; A/B/C=151-301.
DR PDBsum; 5DN4; -.
DR PDBsum; 5DN5; -.
DR AlphaFoldDB; P15931; -.
DR SMR; P15931; -.
DR STRING; 99287.STM1182; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR PaxDb; P15931; -.
DR PRIDE; P15931; -.
DR EnsemblBacteria; AAL20112; AAL20112; STM1182.
DR GeneID; 1252700; -.
DR KEGG; stm:STM1182; -.
DR PATRIC; fig|99287.12.peg.1250; -.
DR HOGENOM; CLU_013771_3_0_6; -.
DR OMA; EGVFVQM; -.
DR PhylomeDB; P15931; -.
DR BioCyc; MetaCyc:STM1182-MON; -.
DR BioCyc; SENT99287:STM1182-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR InterPro; IPR013377; FlaJ.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR SMART; SM00047; LYZ2; 1.
DR TIGRFAMs; TIGR02541; flagell_FlgJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum biogenesis;
KW Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Periplasm;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Peptidoglycan hydrolase FlgJ"
FT /id="PRO_0000165708"
FT REGION 151..316
FT /note="Catalytic"
FT ACT_SITE 223
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /evidence="ECO:0000255"
FT MUTAGEN 223
FT /note="E->Q: Reduced enzymatic activity and poor motility;
FT strongly reduced enzymatic activity and severely attenuated
FT motility; when associated with N-248."
FT /evidence="ECO:0000269|PubMed:10049388"
FT MUTAGEN 248
FT /note="D->N: Reduced enzymatic activity and poor motility."
FT /evidence="ECO:0000269|PubMed:10049388"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:5DN4"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:5DN4"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5DN4"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5DN4"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5DN5"
FT HELIX 285..312
FT /evidence="ECO:0007829|PDB:5DN4"
SQ SEQUENCE 316 AA; 34385 MW; ADD5D5D7AE09607A CRC64;
MIGDGKLLAS AAWDAQSLNE LKAKAGQDPA ANIRPVARQV EGMFVQMMLK SMREALPKDG
LFSSDQTRLY TSMYDQQIAQ QMTAGKGLGL ADMMVKQMTS GQTMPADDAP QVPLKFSLET
VNSYQNQALT QLVRKAIPKT PDSSDAPLSG DSKDFLARLS LPARLASEQS GVPHHLILAQ
AALESGWGQR QILRENGEPS YNVFGVKATA SWKGPVTEIT TTEYENGEAK KVKAKFRVYS
SYLEALSDYV ALLTRNPRYA AVTTAATAEQ GAVALQNAGY ATDPNYARKL TSMIQQLKAM
SEKVSKTYSA NLDNLF
