ID A0A1H4H4H6_9SPHI Unreviewed; 453 AA.
AC A0A1H4H4H6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=SAMN05443550_11318 {ECO:0000313|EMBL:SEB16250.1};
OS Pedobacter hartonius.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=425514 {ECO:0000313|EMBL:SEB16250.1, ECO:0000313|Proteomes:UP000198850};
RN [1] {ECO:0000313|EMBL:SEB16250.1, ECO:0000313|Proteomes:UP000198850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19033 {ECO:0000313|EMBL:SEB16250.1,
RC ECO:0000313|Proteomes:UP000198850};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC Z ring. May serve as a membrane anchor for the Z ring.
CC {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to
CC the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
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DR EMBL; FNRA01000013; SEB16250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4H4H6; -.
DR STRING; 425514.SAMN05443550_11318; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000198850; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.110; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR003494; SHS2_FtsA.
DR NCBIfam; TIGR01174; ftsA; 1.
DR PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR Pfam; PF14450; FtsA; 2.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033};
KW Reference proteome {ECO:0000313|Proteomes:UP000198850}.
FT DOMAIN 13..201
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 453 AA; 49402 MW; 163737B655DAF809 CRC64;
MGKEKTTVQS PIVVGLDIGT TKICVIVGRR TQHGKVEVLG IGKAESAGVT RGVVSNIQKT
VQGISQAVEL ASGQSNVEVR VVNVGIAGQH IKSLQHRGIL TRRELNNEIS KKDLDKLIDD
MFKLVMPPGE EIIHVLPQEF TVDNEPGVKD PIGMAGVRLE ANFHIISGQV TAVKNIMRCV
SNAGLQTQEL ILEPLASSES VLSEEEKEAG IALVDIGGGT TDIAIFHEGI IRHTAVIPFG
GNSVTEDIRE GCSVMRNQAE LLKTRFGSAL AEENKENEII CVPGLRGREP KEISVKNLAY
VIQARMEEII EHVYYEIKSS GYEKKLIGGV VITGGGALLK HLSQLVEYVT GLDCRVGYPN
EHLSKYEDMP KTIYDDLKSP MYATSVGLLI KGIQKAEELI EELKQPGVYV EKPVAAKDKV
KRSGGGLFDK LLAKTKDFIK DDMNVSDEDY IKP
//
