ID M4U2U8_9GAMM Unreviewed; 327 AA.
AC M4U2U8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN Name=flgJ {ECO:0000313|EMBL:AGH80574.1};
GN ORFNames=PCNPT3_03160 {ECO:0000313|EMBL:AGH80574.1};
OS Psychromonas sp. CNPT3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80574.1, ECO:0000313|Proteomes:UP000010320};
RN [1] {ECO:0000313|EMBL:AGH80574.1, ECO:0000313|Proteomes:UP000010320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80574.1,
RC ECO:0000313|Proteomes:UP000010320};
RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA Yayanos A.A., Bartlett D.H.;
RT "The complete genome sequence of the deep-sea bacterium Psychromonas
RT CNPT2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC peptidoglycan layer to assemble the rod structure in the periplasmic
CC space. {ECO:0000256|ARBA:ARBA00002954}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 73 family. {ECO:0000256|ARBA:ARBA00007974}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC {ECO:0000256|ARBA:ARBA00006880}.
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DR EMBL; CP004404; AGH80574.1; -; Genomic_DNA.
DR RefSeq; WP_015464455.1; NC_020802.1.
DR AlphaFoldDB; M4U2U8; -.
DR STRING; 314282.PCNPT3_03160; -.
DR KEGG; psy:PCNPT3_03160; -.
DR eggNOG; COG1705; Bacteria.
DR eggNOG; COG3951; Bacteria.
DR HOGENOM; CLU_013771_3_0_6; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000010320; 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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.70.40; peptidoglycan hydrolase; 1.
DR InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR InterPro; IPR013377; FlaJ.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR NCBIfam; TIGR02541; flagell_FlgJ; 1.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:AGH80574.1};
KW Cilium {ECO:0000313|EMBL:AGH80574.1};
KW Flagellum {ECO:0000313|EMBL:AGH80574.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000010320}.
FT DOMAIN 157..319
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 327 AA; 36210 MW; 831410F20CDF24B2 CRC64;
MSNQSVTPAS NYFDLQGLDQ LRQKALANDK GAIREVANQF EAMFATMLIK SMREANEAFE
TDSPFNNKQT KFYTDMQDKQ LALDISRHGS LGLADALVRQ LDPTSIAGST ESVPLDQLQM
PNTYKTTAFP IEKESTAFAI NQKAAPMEFS MADRAPKVKS SSETLAFTDK KSFINTLLPY
AKKVAKVLGI SPEVLIAQSA LETGWGKKII NDAQNNSSFN LFNIKANASW SGGRVAKESI
EVENGVAVKR RSHFRAYENI AQSFNDYAQF IGQSKRYQGA LEQGTNGSAY IEKLQQAGYA
TDPLYATKVQ SIMQSESFKE ILKEDKN
//
